Publications
2020
Thomès L, Lescure A
Mosaic evolution of the phosphopantothenate biosynthesis pathway in bacteria and archaea Journal Article
In: Genome Biology and Evolution, vol. 13, no. 2, pp. evaa262, 2020.
Abstract | Links | BibTeX | Tags: Candidatus poribacteria, Coenzyme A, LESCURE, phosphopantothenate pathway, Unité ARN
@article{Thomès2020,
title = {Mosaic evolution of the phosphopantothenate biosynthesis pathway in bacteria and archaea},
author = { L Thomès and A Lescure},
url = {https://academic.oup.com/gbe/advance-article/doi/10.1093/gbe/evaa262/6035135},
doi = {10.1093/gbe/evaa262},
year = {2020},
date = {2020-12-15},
journal = {Genome Biology and Evolution},
volume = {13},
number = {2},
pages = {evaa262},
abstract = {Phosphopantothenate is a precursor to synthesis of Coenzyme A (CoA), a molecule essential to many metabolic pathways. Organisms of the archaeal phyla were shown to utilize a different phosphopantothenate biosynthetic pathway from the eukaryotic and bacterial one. In this study, we report that symbiotic bacteria from the group Candidatus poribacteria present enzymes of the archaeal pathway, namely pantoate kinase (PoK) and phosphopantothenate synthetase (PPS), mirroring what was demonstrated for Picrophilus torridus, an archaea partially utilizing the bacterial pathway. Our results support the ancient origin of the CoA pathway in the three domains of life, but also highlight its complex and dynamic evolution. Importantly, this study helps to improve protein annotation for this pathway in the Candidatus poribacteria group and other related organisms.},
keywords = {Candidatus poribacteria, Coenzyme A, LESCURE, phosphopantothenate pathway, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Despons L, Martin F
How Many Messenger RNAs Can Be Translated by the START Mechanism? Journal Article
In: International Journal of Molecular Sciences, vol. 21, no. 21, pp. 8373, 2020.
Abstract | Links | BibTeX | Tags: ERIANI, LESCURE, mRNA, Ribosome, secondary structures, START, translation initiation, Unité ARN
@article{Despons2020,
title = {How Many Messenger RNAs Can Be Translated by the START Mechanism? },
author = {L Despons and F Martin
},
url = {https://pubmed.ncbi.nlm.nih.gov/33171614/},
doi = {10.3390/ijms21218373 },
year = {2020},
date = {2020-11-01},
journal = {International Journal of Molecular Sciences},
volume = {21},
number = {21},
pages = {8373},
abstract = {Translation initiation is a key step in the protein synthesis stage of the gene expression pathway of all living cells. In this important process, ribosomes have to accurately find the AUG start codon in order to ensure the integrity of the proteome. "Structure Assisted RNA Translation", or "START", has been proposed to use stable secondary structures located in the coding sequence to augment start site selection by steric hindrance of the progression of pre-initiation complex on messenger RNA. This implies that such structures have to be located downstream and at on optimal distance from the AUG start codon (i.e., downstream nucleotide +16). In order to assess the importance of the START mechanism in the overall mRNA translation process, we developed a bioinformatic tool to screen coding sequences for such stable structures in a 50 nucleotide-long window spanning the nucleotides from +16 to +65. We screened eight bacterial genomes and six eukaryotic genomes. We found stable structures in 0.6-2.5% of eukaryotic coding sequences. Among these, approximately half of them were structures predicted to form G-quadruplex structures. In humans, we selected 747 structures. In bacteria, the coding sequences from Gram-positive bacteria contained 2.6-4.2% stable structures, whereas the structures were less abundant in Gram-negative bacteria (0.2-2.7%). In contrast to eukaryotes, putative G-quadruplex structures are very rare in the coding sequence of bacteria. Altogether, our study reveals that the START mechanism seems to be an ancient strategy to facilitate the start codon recognition that is used in different kingdoms of life. },
keywords = {ERIANI, LESCURE, mRNA, Ribosome, secondary structures, START, translation initiation, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Chernorudskiy A, Varone E, Colombo S F, Fumagalli S, Cagnotto A, Cattaneo A, Briens M, Baltzinger M, Kuhn L, Bachi A, Berardi A, Salmona M, Musco G, Borgese N, Lescure A, Zito E
Selenoprotein N is an endoplasmic reticulum calcium sensor that links luminal calcium levels to a redox activity Journal Article
In: Proc Natl Acad Sci U S A, vol. 117, no. 35, pp. 21288-21298, 2020, ISBN: 32817544.
Abstract | Links | BibTeX | Tags: LESCURE, PPSE, Unité ARN
@article{,
title = {Selenoprotein N is an endoplasmic reticulum calcium sensor that links luminal calcium levels to a redox activity},
author = {A Chernorudskiy and E Varone and S F Colombo and S Fumagalli and A Cagnotto and A Cattaneo and M Briens and M Baltzinger and L Kuhn and A Bachi and A Berardi and M Salmona and G Musco and N Borgese and A Lescure and E Zito},
url = {https://pubmed.ncbi.nlm.nih.gov/32817544/},
doi = {10.1073/pnas.2003847117},
isbn = {32817544},
year = {2020},
date = {2020-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {117},
number = {35},
pages = {21288-21298},
abstract = {The endoplasmic reticulum (ER) is the reservoir for calcium in cells. Luminal calcium levels are determined by calcium-sensing proteins that trigger calcium dynamics in response to calcium fluctuations. Here we report that Selenoprotein N (SEPN1) is a type II transmembrane protein that senses ER calcium fluctuations by binding this ion through a luminal EF-hand domain. In vitro and in vivo experiments show that via this domain, SEPN1 responds to diminished luminal calcium levels, dynamically changing its oligomeric state and enhancing its redox-dependent interaction with cellular partners, including the ER calcium pump sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA). Importantly, single amino acid substitutions in the EF-hand domain of SEPN1 identified as clinical variations are shown to impair its calcium-binding and calcium-dependent structural changes, suggesting a key role of the EF-hand domain in SEPN1 function. In conclusion, SEPN1 is a ER calcium sensor that responds to luminal calcium depletion, changing its oligomeric state and acting as a reductase to refill ER calcium stores.},
keywords = {LESCURE, PPSE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2019
Janvier A, Despons L, Schaeffer L, Tidu A, Martin F, Eriani G
A tRNA-mimic Strategy to Explore the Role of G34 of tRNAGly in Translation and Codon Frameshifting Journal Article
In: Int J Mol Sci, vol. 20, no. 16, pp. 3911, 2019, ISBN: 31405256.
Abstract | Links | BibTeX | Tags: ERIANI, IRES element frameshifting genetic code glycine codon tRNA translation, LESCURE, Unité ARN
@article{,
title = {A tRNA-mimic Strategy to Explore the Role of G34 of tRNA^{Gly} in Translation and Codon Frameshifting},
author = {A Janvier and L Despons and L Schaeffer and A Tidu and F Martin and G Eriani},
url = {https://www.ncbi.nlm.nih.gov/pubmed/31405256?dopt=Abstract},
doi = {10.3390/ijms20163911},
isbn = {31405256},
year = {2019},
date = {2019-01-01},
journal = {Int J Mol Sci},
volume = {20},
number = {16},
pages = {3911},
abstract = {Decoding of the 61 sense codons of the genetic code requires a variable number of tRNAs that establish codon-anticodon interactions. Thanks to the wobble base pairing at the third codon position, less than 61 different tRNA isoacceptors are needed to decode the whole set of codons. On the tRNA, a subtle distribution of nucleoside modifications shapes the anticodon loop structure and participates to accurate decoding and reading frame maintenance. Interestingly, although the 61 anticodons should exist in tRNAs, a strict absence of some tRNAs decoders is found in several codon families. For instance, in Eukaryotes, G34-containing tRNAs translating 3-, 4- and 6-codon boxes are absent. This includes tRNA specific for Ala, Arg, Ile, Leu, Pro, Ser, Thr, and Val. tRNAGly is the only exception for which in the three kingdoms, a G34-containing tRNA exists to decode C3 and U3-ending codons. To understand why G34-tRNAGly exists, we analysed at the genome wide level the codon distribution in codon +1 relative to the four GGN Gly codons. When considering codon GGU, a bias was found towards an unusual high usage of codons starting with a G whatever the amino acid at +1 codon. It is expected that GGU codons are decoded by G34-containing tRNAGly, decoding also GGC codons. Translation studies revealed that the presence of a G at the first position of the downstream codon reduces the +1 frameshift by stabilizing the G34U3 wobble interaction. This result partially explains why G34-containing tRNAGly exists in Eukaryotes whereas all the other G34-containing tRNAs for multiple codon boxes are absent.},
keywords = {ERIANI, IRES element frameshifting genetic code glycine codon tRNA translation, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2018
Paulson R F, Nettleford S, Liao C, Chen Y, Hao S, Baltzinger M, Thami-Braye M, Lescure A, Prabhu K S
The role of Selenoprotein N in the differentiation of erythroid progenitors during stress erythropoiesis Miscellaneous
2018.
Abstract | BibTeX | Tags: LESCURE, Unité ARN
@misc{,
title = {The role of Selenoprotein N in the differentiation of erythroid progenitors during stress erythropoiesis},
author = {R F Paulson and S Nettleford and C Liao and Y Chen and S Hao and M Baltzinger and M Thami-Braye and A Lescure and K S Prabhu},
year = {2018},
date = {2018-01-01},
number = {Dec 25},
publisher = {BioRxiv 528638 [Preprint]},
abstract = {Low serum Se is independently associated with anemia in elderly population, dialysis patients, sickle-cells patients, and hypothyroidism patients. Previous work from our laboratory showed that dietary Se deficiency in mice showed mild anemia indicating activation of stress-erythropoietic mechanisms. Unlike steady state erythropoiesis that is primarily responsible for homeostasis to produce new erythrocytes at a constant rate, stress erythropoiesis predominates when the bone marrow cannot generate sufficient erythrocytes. During such a process, short-term reconstituting hematopoietic stem cells (CD34+Kit+Sca1+Linneg) migrate to the spleen leading to the proliferation and differentiation of stress-erythroid progenitors (SEPs). These cells lead to stress burst forming unit-erythroid cells (BFU-E) followed by terminal differentiation to erythrocytes. Recent studies demonstrate deficits in selenoproteins block the expansion and development of stress BFU-E with defects in terminal differentiation. Analysis of selenoprotein expression showed that selenoprotein W (SelenoW) was highly expressed in developing SEPs. CRISPR-Cas9 knockout of SelenoW blocked the proliferation of immature SEPs in murine and human stress erythropoiesis cultures demonstrating a central role for SelenoW in stress erythropoiesis. Using the two-culture system to generate SEPs, selenoprotein N (SelenoN) expression increased as the progenitors transition from self-renewing モstem cell likeヤ progenitors to form committed erythroid progenitors. SelenoN−/− mice showed significantly slower erythroid recovery following phenylhydrazine (PHZ)-induced acute hemolytic anemia. As in the muscle satellite cells where SelenoN regulates cellular Ca2+ signaling, SelenoN may also regulate Ca2+ signaling in SEPs to modulate pathways of differentiation. In summary, these data suggest that multiple selenoproteins, including SelenoN and SelenoW, coordinately regulate stress erythropoiesis.},
keywords = {LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {misc}
}
Lescure A, Baltzinger M, Zito E
Uncovering the Importance of Selenium in Muscle Disease Book Chapter
In: Michalke, B (Ed.): Selenium: Series Molecular and Integrative Toxicology, pp. 345-362, Springer, New-York, 2018.
Abstract | Links | BibTeX | Tags: elenium Selenoproteins Muscle disease Oxidative stress Calcium transport RYR SERCA, LESCURE, Unité ARN
@inbook{,
title = {Uncovering the Importance of Selenium in Muscle Disease},
author = {A Lescure and M Baltzinger and E Zito},
editor = {B Michalke},
url = {https://link.springer.com/chapter/10.1007/978-3-319-95390-8_18},
doi = {978-3-319-95390-8_18},
year = {2018},
date = {2018-01-01},
booktitle = {Selenium: Series Molecular and Integrative Toxicology},
pages = {345-362},
publisher = {Springer},
address = {New-York},
series = {Molecular and Integrative Toxicology},
abstract = {A connection between selenium bioavailability and development of muscular disorders both in humans and livestock has been established for a long time. With the development of genomics, the function of several selenoproteins was shown to be involved in muscle activity, including SELENON, which was linked to an inherited form of myopathy. Development of animal models has helped to dissect the physiological dysfunction due to mutation in the SELENON gene; however the molecular activity remains elusive and only recent analysis using both in vivo and in vitro experiment provided hints toward its function in oxidative stress defence and calcium transport control. This review sets out to summarise most recent findings for the importance of selenium in muscle function and the contribution of this information to the design of strategies to cure the diseases.},
keywords = {elenium Selenoproteins Muscle disease Oxidative stress Calcium transport RYR SERCA, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {inbook}
}
Smyth R. P., Smith M. R., Jousset A. C., Despons L., Laumond G., Decoville T., Cattenoz P., Moog C., Jossinet F., Mougel M., Paillart J. C., Kleist M., Marquet R.
In: Nucleic Acids Res, vol. 46, no. 9, pp. e57, 2018, ISBN: 29514260, (1362-4962 (Electronic) 0305-1048 (Linking) Journal Article Research Support, Non-U.S. Gov't).
Abstract | Links | BibTeX | Tags: 5' Untranslated Regions Genome, LESCURE, Ribonucleic Acid *Virus Assembly Virus Replication, Unité ARN, Viral HEK293 Cells HIV-1/*genetics/physiology Humans Mutation Nucleotide Motifs Poly A/metabolism RNA, Viral/*biosynthesis/*chemistry *Regulatory Sequences
@article{nokey,
title = {In cell mutational interference mapping experiment (in cell MIME) identifies the 5' polyadenylation signal as a dual regulator of HIV-1 genomic RNA production and packaging},
author = {R. P. Smyth and M. R. Smith and A. C. Jousset and L. Despons and G. Laumond and T. Decoville and P. Cattenoz and C. Moog and F. Jossinet and M. Mougel and J. C. Paillart and M. Kleist and R. Marquet},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=29514260},
doi = {10.1093/nar/gky152},
isbn = {29514260},
year = {2018},
date = {2018-01-01},
journal = {Nucleic Acids Res},
volume = {46},
number = {9},
pages = {e57},
abstract = {Non-coding RNA regulatory elements are important for viral replication, making them promising targets for therapeutic intervention. However, regulatory RNA is challenging to detect and characterise using classical structure-function assays. Here, we present in cell Mutational Interference Mapping Experiment (in cell MIME) as a way to define RNA regulatory landscapes at single nucleotide resolution under native conditions. In cell MIME is based on (i) random mutation of an RNA target, (ii) expression of mutated RNA in cells, (iii) physical separation of RNA into functional and non-functional populations, and (iv) high-throughput sequencing to identify mutations affecting function. We used in cell MIME to define RNA elements within the 5' region of the HIV-1 genomic RNA (gRNA) that are important for viral replication in cells. We identified three distinct RNA motifs controlling intracellular gRNA production, and two distinct motifs required for gRNA packaging into virions. Our analysis reveals the 73AAUAAA78 polyadenylation motif within the 5' PolyA domain as a dual regulator of gRNA production and gRNA packaging, and demonstrates that a functional polyadenylation signal is required for viral packaging even though it negatively affects gRNA production.},
note = {1362-4962 (Electronic)
0305-1048 (Linking)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {5' Untranslated Regions Genome, LESCURE, Ribonucleic Acid *Virus Assembly Virus Replication, Unité ARN, Viral HEK293 Cells HIV-1/*genetics/physiology Humans Mutation Nucleotide Motifs Poly A/metabolism RNA, Viral/*biosynthesis/*chemistry *Regulatory Sequences},
pubstate = {published},
tppubtype = {article}
}
2016
Lescure A, Briens M, Ferreiro A
What do we know about selenium contribution to muscle physiology? Book Chapter
In: Hatfield, D L; Schweizer, U; Tsuji, P A; Gladyshev, V (Ed.): Selenium: Its molecular biology and role in human health, pp. 475-486, Springer, 4, 2016.
Abstract | Links | BibTeX | Tags: Intracellular calcium handling Muscle Muscular dystrophies Oxidative stress Selenium Selenoprotein N, LESCURE, Unité ARN
@inbook{,
title = {What do we know about selenium contribution to muscle physiology?},
author = {A Lescure and M Briens and A Ferreiro},
editor = {D L Hatfield and U Schweizer and P A Tsuji and V Gladyshev},
url = {http://link.springer.com/chapter/10.1007/978-3-319-41283-2_40},
doi = {10.1007/978-3-319-41283-2_40},
year = {2016},
date = {2016-01-01},
booktitle = {Selenium: Its molecular biology and role in human health},
pages = {475-486},
publisher = {Springer},
edition = {4},
abstract = {Early observations of selenium (Se) deficiencies in human and livestock revealed the importance of this trace element for normal muscle function. However, the molecular and cellular dysfunction connecting low selenium diets to muscular diseases remain elusive. Importantly, mutations in the SEPN1 gene encoding selenoprotein N (SEPN1) were shown to cause an inherited muscular disease in humans. Therefore, it is expected that understanding the role of SEPN1 and the related pathophysiology will unveil the participation of Se in molecular processes essential for muscle function and pave the way for targeted therapeutics. However, the functional characterization of SEPN1 is still lacking. Analysis of its activity in cellular and animal models pointed to its involvement in oxidative stress defense and in control of calcium (Ca2+) handling. A link between the activities of SEPN1 and of the Ca2+ transporters, RyR1 and SERCA, was shown, but the enzymatic reaction catalyzed by SEPN1 has not been characterized.},
keywords = {Intracellular calcium handling Muscle Muscular dystrophies Oxidative stress Selenium Selenoprotein N, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {inbook}
}
Gladyshev V N, Arnér E S, Berry M J, Brigelius-Flohé R, Bruford E A, Burk R F, Carlson B A, Castellano S, Chavatte L, Conrad M, Copeland P R, Diamond A M, Driscoll D M, Ferreiro A, Flohé L, Green F R, Guigó R, Handy D E, Hatfield D L, Hesketh J, Hoffmann P R, Holmgren A, Hondal R J, Howard M T, Huang K, Kim H Y, Kim I Y, Köhrle J, Krol A, Kryukov G V, Lee B J, Lee B C, Lei X G, Liu Q, Lescure A, Lobanov A V, Loscalzo J, Maiorino M, Mariotti M, Prabhu K S, Rayman M P, Rozovsky S, Salinas G, Schomburg L, Schweizer U, Simonović M, Sunde R A, Tsuji P A, Tweedie S, Ursini F, Zhang Y
Selenoprotein Gene Nomenclature. Journal Article
In: J Biol Chem, vol. 291, no. 46, pp. 24036-24040, 2016, ISBN: 27645994.
Abstract | Links | BibTeX | Tags: function gene name genomics nomenclature selenium selenocysteine selenoprotein structure-function, LESCURE, Unité ARN
@article{,
title = {Selenoprotein Gene Nomenclature.},
author = {V N Gladyshev and E S Arnér and M J Berry and R Brigelius-Flohé and E A Bruford and R F Burk and B A Carlson and S Castellano and L Chavatte and M Conrad and P R Copeland and A M Diamond and D M Driscoll and A Ferreiro and L Flohé and F R Green and R Guigó and D E Handy and D L Hatfield and J Hesketh and P R Hoffmann and A Holmgren and R J Hondal and M T Howard and K Huang and H Y Kim and I Y Kim and J Köhrle and A Krol and G V Kryukov and B J Lee and B C Lee and X G Lei and Q Liu and A Lescure and A V Lobanov and J Loscalzo and M Maiorino and M Mariotti and K S Prabhu and M P Rayman and S Rozovsky and G Salinas and L Schomburg and U Schweizer and M Simonović and R A Sunde and P A Tsuji and S Tweedie and F Ursini and Y Zhang},
url = {https://www.ncbi.nlm.nih.gov/pubmed/27645994?dopt=Abstract},
doi = {10.1074/jbc.M116.756155},
isbn = {27645994},
year = {2016},
date = {2016-01-01},
journal = {J Biol Chem},
volume = {291},
number = {46},
pages = {24036-24040},
abstract = {The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions are designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4 and GPX6 (glutathione peroxidases), DIO1, DIO2, and DIO3 (iodothyronine deiodinases), MSRB1 (methionine-R-sulfoxide reductase 1) and SEPHS2 (selenophosphate synthetase 2). Selenoproteins without known functions have traditionally been denoted by SEL or SEP symbols. However, these symbols are sometimes ambiguous and conflict with the approved nomenclature for several other genes. Therefore, there is a need to implement a rational and coherent nomenclature system for selenoprotein-encoding genes. Our solution is to use the root symbol SELENO followed by a letter. This nomenclature applies to SELENOF (selenoprotein F, the 15 kDa selenoprotein, SEP15), SELENOH (selenoprotein H, SELH, C11orf31), SELENOI (selenoprotein I, SELI, EPT1), SELENOK (selenoprotein K, SELK), SELENOM (selenoprotein M, SELM), SELENON (selenoprotein N, SEPN1, SELN), SELENOO (selenoprotein O, SELO), SELENOP (selenoprotein P, SeP, SEPP1, SELP), SELENOS (selenoprotein S, SELS, SEPS1, VIMP), SELENOT (selenoprotein T, SELT), SELENOV (selenoprotein V, SELV) and SELENOW (selenoprotein W, SELW, SEPW1). This system, approved by the HUGO Gene Nomenclature Committee, also resolves conflicting, missing and ambiguous designations for selenoprotein genes and is applicable to selenoproteins across vertebrates.},
keywords = {function gene name genomics nomenclature selenium selenocysteine selenoprotein structure-function, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Guedich S, Puffer-Enders B, Baltzinger M, Hoffmann G, Veiga C Da, Jossinet F, Thore S, Bec G, Ennifar E, Burnouf D, Dumas P
Quantitative and predictive model of kinetic regulation by E. coli TPP riboswitches. Journal Article
In: RNA Biol, vol. 13, no. 4, pp. 373-390, 2016, ISBN: 26932506.
Abstract | Links | BibTeX | Tags: ENNIFAR, Kinetic Regulation kinITC pyrophosphate riboswitches thiamine, LESCURE, Unité ARN
@article{,
title = {Quantitative and predictive model of kinetic regulation by E. coli TPP riboswitches.},
author = {S Guedich and B Puffer-Enders and M Baltzinger and G Hoffmann and C Da Veiga and F Jossinet and S Thore and G Bec and E Ennifar and D Burnouf and P Dumas},
url = {http://www.ncbi.nlm.nih.gov/pubmed/26932506?dopt=Abstract},
doi = {10.1080/15476286.2016.1142040},
isbn = {26932506},
year = {2016},
date = {2016-01-01},
journal = {RNA Biol},
volume = {13},
number = {4},
pages = {373-390},
abstract = {Riboswitches are non-coding elements upstream or downstream of mRNAs that, upon binding of a specific ligand, regulate transcription and/or translation initiation in bacteria, or alternative splicing in plants and fungi. We have studied thiamine pyrophosphate (TPP) riboswitches regulating translation of thiM operon and transcription and translation of thiC operon in E. coli, and that of THIC in the plant A. thaliana. For all, we ascertained an induced-fit mechanism involving initial binding of the TPP followed by a conformational change leading to a higher-affinity complex. The experimental values obtained for all kinetic and thermodynamic parameters of TPP binding imply that the regulation by A. thaliana riboswitch is governed by mass-action law, whereas it is of kinetic nature for the two bacterial riboswitches. Kinetic regulation requires that the RNA polymerase pauses after synthesis of each riboswitch aptamer to leave time for TPP binding, but only when its concentration is sufficient. A quantitative model of regulation highlighted how the pausing time has to be linked to the kinetic rates of initial TPP binding to obtain an ON/OFF switch in the correct concentration range of TPP. We verified the existence of these pauses and the model prediction on their duration. Our analysis also led to quantitative estimates of the respective efficiency of kinetic and thermodynamic regulations, which shows that kinetically regulated riboswitches react more sharply to concentration variation of their ligand than thermodynamically regulated riboswitches. This rationalizes the interest of kinetic regulation and confirms empirical observations that were obtained by numerical simulations.},
keywords = {ENNIFAR, Kinetic Regulation kinITC pyrophosphate riboswitches thiamine, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2012
Lescure A, Castets P, Grunwald D, Allamand V, Howard M
Selenoprotein N: Its role in disease. Book Chapter
In: Hatfield, D; Berry, M; Gladyshev, V (Ed.): Selenium: Its molecular biology and role in human health, pp. 283-294, Springer, 2, 2012.
Abstract | Links | BibTeX | Tags: KROL, LESCURE, Unité ARN
@inbook{,
title = {Selenoprotein N: Its role in disease.},
author = {A Lescure and P Castets and D Grunwald and V Allamand and M Howard},
editor = {D Hatfield and M Berry and V Gladyshev},
url = {http://www.springerlink.com/content/h457r0g274533522/},
doi = {10.1007/978-1-4614-1025-6_22},
year = {2012},
date = {2012-01-01},
booktitle = {Selenium: Its molecular biology and role in human health},
pages = {283-294},
publisher = {Springer},
edition = {2},
abstract = {Selenoprotein N is among the newly identified selenoproteins, initially discovered in silico with no known molecular function. It has become the focus of attention because mutations in the selenoprotein N gene are linked to a group of muscle disorders, now referred as SEPN1-related myopathies. An emerging view arising from recent findings is that the loss of selenoprotein N leads to cellular sensitivity to oxidative stress and loss of calcium homeostasis. Studies of animal models for SEPN1-Related Myopathies revealed the fate of sensitized muscle may depend on stresses to which it is subjected, and defects in the function of selenoprotein N-deficient muscle progenitor cells during development in zebrafish embryos or during muscle regeneration in fully developed mouse muscle. Dysfunction of these different processes raises significant questions regarding which of the phenotypic manifestations of SEPN1-Related Myopathies are initiated by events during development and which are progressive in nature arising from dysfunction of mature muscle.},
keywords = {KROL, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {inbook}
}
2011
Rudinger-Thirion J, Lescure A, Paulus C, Frugier M
Misfolded human tRNA isodecoder binds and neutralizes a 3' UTR-embedded Alu element Journal Article
In: Proc Natl Acad Sci U S A, vol. 108, no. 40, pp. E794-802, 2011, ISSN: 1091-6490 (Electronic) 0027-8424 (Linking), (Rudinger-Thirion, Joelle Lescure, Alain Paulus, Caroline Frugier, Magali United States Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 2011 Oct 4;108(40):E794-802. Epub 2011 Sep 6.).
Abstract | Links | BibTeX | Tags: FRUGIER, LESCURE, Unité ARN
@article{,
title = {Misfolded human tRNA isodecoder binds and neutralizes a 3' UTR-embedded Alu element},
author = {J Rudinger-Thirion and A Lescure and C Paulus and M Frugier},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=21896722},
doi = {10.1073/pnas.1103698108},
issn = {1091-6490 (Electronic) 0027-8424 (Linking)},
year = {2011},
date = {2011-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {108},
number = {40},
pages = {E794-802},
abstract = {Several classes of small noncoding RNAs are key players in cellular metabolism including mRNA decoding, RNA processing, and mRNA stability. Here we show that a tRNA(Asp) isodecoder, corresponding to a human tRNA-derived sequence, binds to an embedded Alu RNA element contained in the 3' UTR of the human aspartyl-tRNA synthetase mRNA. This interaction between two well-known classes of RNA molecules, tRNA and Alu RNA, is driven by an unexpected structural motif and induces a global rearrangement of the 3' UTR. Besides, this 3' UTR contains two functional polyadenylation signals. We propose a model where the tRNA/Alu interaction would modulate the accessibility of the two alternative polyadenylation sites and regulate the stability of the mRNA. This unique regulation mechanism would link gene expression to RNA polymerase III transcription and may have implications in a primate-specific signal pathway.},
note = {Rudinger-Thirion, Joelle
Lescure, Alain
Paulus, Caroline
Frugier, Magali
United States
Proceedings of the National Academy of Sciences of the United States of America
Proc Natl Acad Sci U S A. 2011 Oct 4;108(40):E794-802. Epub 2011 Sep 6.},
keywords = {FRUGIER, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Rederstorff M, Castets P, Arbogast S, Lainé J, Vassilopoulos S, Beuvin M, Dubourg O, Vignaud A, Ferry A, Krol A, Allamand V, Guicheney P, Ferreiro A, Lescure A
Increased muscle stress-sensitivity induced by selenoprotein N inactivation in mouse: a mammalian model for SEPN1-related myopathy. Journal Article
In: PLoS One, vol. 6, no. 8, pp. e23094, 2011, ISBN: 21858002.
Abstract | Links | BibTeX | Tags: KROL, LESCURE, Unité ARN
@article{,
title = {Increased muscle stress-sensitivity induced by selenoprotein N inactivation in mouse: a mammalian model for SEPN1-related myopathy.},
author = {M Rederstorff and P Castets and S Arbogast and J Lainé and S Vassilopoulos and M Beuvin and O Dubourg and A Vignaud and A Ferry and A Krol and V Allamand and P Guicheney and A Ferreiro and A Lescure},
url = {http://www.ncbi.nlm.nih.gov/pubmed/21858002},
doi = {10.1371/journal.pone.0023094},
isbn = {21858002},
year = {2011},
date = {2011-01-01},
journal = {PLoS One},
volume = {6},
number = {8},
pages = {e23094},
abstract = {Selenium is an essential trace element and selenoprotein N (SelN) was the first selenium-containing protein shown to be directly involved in human inherited diseases. Mutations in the SEPN1 gene, encoding SelN, cause a group of muscular disorders characterized by predominant affection of axial muscles. SelN has been shown to participate in calcium and redox homeostasis, but its pathophysiological role in skeletal muscle remains largely unknown. To address SelN function in vivo, we generated a Sepn1-null mouse model by gene targeting. The Sepn1(-/-) mice had normal growth and lifespan, and were macroscopically indistinguishable from wild-type littermates. Only minor defects were observed in muscle morphology and contractile properties in SelN-deficient mice in basal conditions. However, when subjected to challenging physical exercise and stress conditions (forced swimming test), Sepn1(-/-) mice developed an obvious phenotype, characterized by limited motility and body rigidity during the swimming session, as well as a progressive curvature of the spine and predominant alteration of paravertebral muscles. This induced phenotype recapitulates the distribution of muscle involvement in patients with SEPN1-Related Myopathy, hence positioning this new animal model as a valuable tool to dissect the role of SelN in muscle function and to characterize the pathophysiological process},
keywords = {KROL, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2009
Lescure A, Rederstorff M, Krol A, Guicheney P, Allamand V
Selenoprotein function and muscle disease Journal Article
In: Biochim Biophys Acta-Gen Subj, vol. 1790, no. 11, pp. 1569-1574, 2009, ISBN: 19285112, (0006-3002 (Print) 0006-3002 (Linking) Journal Article Research Support, Non-U.S. Gov't Review).
Abstract | Links | BibTeX | Tags: Biological Muscle Proteins/genetics/physiology Muscles/physiology Muscular Diseases/*etiology/genetics Mutation/physiology Selenoproteins/genetics/*physiology, KROL Animals Calcium/metabolism Humans Intracellular Fluid/metabolism Models, LESCURE, Unité ARN
@article{,
title = {Selenoprotein function and muscle disease},
author = {A Lescure and M Rederstorff and A Krol and P Guicheney and V Allamand},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19285112},
isbn = {19285112},
year = {2009},
date = {2009-01-01},
journal = {Biochim Biophys Acta-Gen Subj},
volume = {1790},
number = {11},
pages = {1569-1574},
abstract = {The crucial role of the trace element selenium in livestock and human health, in particular in striated muscle function, has been well established but the underlying molecular mechanisms remain poorly understood. Over the last decade, identification of the full repertoire of selenium-containing proteins has opened the way towards a better characterization of these processes. Two selenoproteins have mainly been investigated in muscle, namely SelW and SelN. Here we address their involvement in muscle development and maintenance, through the characterization of various cellular or animal models. In particular, mutations in the SEPN1 gene encoding selenoprotein N (SelN) cause a group of neuromuscular disorders now referred to as SEPN1-related myopathy. Recent findings on the functional consequences of these mutations suggest an important contribution of SelN to the regulation of oxidative stress and calcium homeostasis. Importantly, the conclusions of these experiments have opened new avenues of investigations that provide grounds for the development of therapeutic approaches.},
note = {0006-3002 (Print)
0006-3002 (Linking)
Journal Article
Research Support, Non-U.S. Gov't
Review},
keywords = {Biological Muscle Proteins/genetics/physiology Muscles/physiology Muscular Diseases/*etiology/genetics Mutation/physiology Selenoproteins/genetics/*physiology, KROL Animals Calcium/metabolism Humans Intracellular Fluid/metabolism Models, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Castets P, Maugenre S, Gartioux C, Rederstorff M, Krol A, Lescure A, Tajbakhsh S, Allamand V, Guicheney P
Selenoprotein N is dynamically expressed during mouse development and detected early in muscle precursors Journal Article
In: BMC Dev Biol, vol. 9, pp. 46, 2009, ISBN: 19698141, (1471-213X (Electronic) 1471-213X (Linking) Journal Article Research Support, Non-U.S. Gov't).
Abstract | Links | BibTeX | Tags: Developmental Humans Mice Muscle Proteins/genetics/*metabolism Muscle, KROL Animals Embryo, LESCURE, Mammalian/metabolism *Gene Expression Regulation, Skeletal/*embryology Myoblasts/metabolism Ryanodine Receptor Calcium Release Channel/metabolism Selenoproteins/genetics/*metabolism Zebrafish/embryology, Unité ARN
@article{,
title = {Selenoprotein N is dynamically expressed during mouse development and detected early in muscle precursors},
author = {P Castets and S Maugenre and C Gartioux and M Rederstorff and A Krol and A Lescure and S Tajbakhsh and V Allamand and P Guicheney},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19698141},
isbn = {19698141},
year = {2009},
date = {2009-01-01},
journal = {BMC Dev Biol},
volume = {9},
pages = {46},
abstract = {BACKGROUND: In humans, mutations in the SEPN1 gene, encoding selenoprotein N (SelN), are involved in early onset recessive neuromuscular disorders, referred to as SEPN1-related-myopathies. The mechanisms behind these pathologies are poorly understood since the function of SelN remains elusive. However, previous results obtained in humans and more recently in zebrafish pointed to a potential role for SelN during embryogenesis. Using qRT-PCR, Western blot and whole mount in situ hybridization, we characterized in detail the spatio-temporal expression pattern of the murine Sepn1 gene during development, focusing particularly on skeletal muscles. RESULTS: In whole embryos, Sepn1 transcripts were detected as early as E5.5, with expression levels peaking at E12.5, and then strongly decreasing until birth. In isolated tissues, only mild transcriptional variations were observed during development, whereas a striking reduction of the protein expression was detected during the perinatal period. Furthermore, we demonstrated that Sepn1 is expressed early in somites and restricted to the myotome, the sub-ectodermal mesenchyme and the dorsal root ganglia at mid-gestation stages. Interestingly, Sepn1 deficiency did not alter somitogenesis in embryos, suggesting that SelN is dispensable for these processes in mouse. CONCLUSION: We characterized for the first time the expression pattern of Sepn1 during mammalian embryogenesis and we demonstrated that its differential expression is most likely dependent on major post-transcriptional regulations. Overall, our data strongly suggest a potential role for selenoprotein N from mid-gestation stages to the perinatal period. Interestingly, its specific expression pattern could be related to the current hypothesis that selenoprotein N may regulate the activity of the ryanodine receptors.},
note = {1471-213X (Electronic)
1471-213X (Linking)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {Developmental Humans Mice Muscle Proteins/genetics/*metabolism Muscle, KROL Animals Embryo, LESCURE, Mammalian/metabolism *Gene Expression Regulation, Skeletal/*embryology Myoblasts/metabolism Ryanodine Receptor Calcium Release Channel/metabolism Selenoproteins/genetics/*metabolism Zebrafish/embryology, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2008
Rederstorff M, Allamand V, Guicheney P, Gartioux C, Richard P, Chaigne D, Krol A, Lescure A
Ex vivo correction of selenoprotein N deficiency in rigid spine muscular dystrophy caused by a mutation in the selenocysteine codon Journal Article
In: Nucleic Acids Res, vol. 36, no. 1, pp. 237-244, 2008, ISBN: 18025044, (1362-4962 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Abstract | Links | BibTeX | Tags: Amino Acid-Specific/*genetics Selenocysteine/metabolism Selenoproteins/biosynthesis/*deficiency/*genetics Transgenes, KROL Codon/chemistry *Codon, LESCURE, Nonsense Fibroblasts/metabolism Hela Cells Humans Muscle Proteins/biosynthesis/*deficiency/*genetics Muscular Atrophy, Spinal/*genetics/metabolism RNA, Transfer, Unité ARN
@article{,
title = {Ex vivo correction of selenoprotein N deficiency in rigid spine muscular dystrophy caused by a mutation in the selenocysteine codon},
author = {M Rederstorff and V Allamand and P Guicheney and C Gartioux and P Richard and D Chaigne and A Krol and A Lescure},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18025044},
isbn = {18025044},
year = {2008},
date = {2008-01-01},
journal = {Nucleic Acids Res},
volume = {36},
number = {1},
pages = {237-244},
abstract = {Premature termination of translation due to nonsense mutations is a frequent cause of inherited diseases. Therefore, many efforts were invested in the development of strategies or compounds to selectively suppress this default. Selenoproteins are interesting candidates considering the idiosyncrasy of the amino acid selenocysteine (Sec) insertion mechanism. Here, we focused our studies on SEPN1, a selenoprotein gene whose mutations entail genetic disorders resulting in different forms of muscular diseases. Selective correction of a nonsense mutation at the Sec codon (UGA to UAA) was undertaken with a corrector tRNA(Sec) that was engineered to harbor a compensatory mutation in the anticodon. We demonstrated that its expression restored synthesis of a full-length selenoprotein N both in HeLa cells and in skin fibroblasts from a patient carrying the mutated Sec codon. Readthrough of the UAA codon was effectively dependent on the Sec insertion machinery, therefore being highly selective for this gene and unlikely to generate off-target effects. In addition, we observed that expression of the corrector tRNA(Sec) stabilized the mutated SEPN1 transcript that was otherwise more subject to degradation. In conclusion, our data provide interesting evidence that premature termination of translation due to nonsense mutations is amenable to correction, in the context of the specialized selenoprotein synthesis mechanism.},
note = {1362-4962 (Electronic)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {Amino Acid-Specific/*genetics Selenocysteine/metabolism Selenoproteins/biosynthesis/*deficiency/*genetics Transgenes, KROL Codon/chemistry *Codon, LESCURE, Nonsense Fibroblasts/metabolism Hela Cells Humans Muscle Proteins/biosynthesis/*deficiency/*genetics Muscular Atrophy, Spinal/*genetics/metabolism RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Deniziak M, Rederstorff M, Krol A
Molecular basis for the role of selenium in muscle development and function Journal Article
In: Chem Biodivers, vol. 5, no. 3, pp. 408-413, 2008, ISBN: 18357550, (1612-1880 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Links | BibTeX | Tags: KROL, LESCURE, Unité ARN
@article{,
title = {Molecular basis for the role of selenium in muscle development and function},
author = {A Lescure and M Deniziak and M Rederstorff and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18357550},
isbn = {18357550},
year = {2008},
date = {2008-01-01},
journal = {Chem Biodivers},
volume = {5},
number = {3},
pages = {408-413},
note = {1612-1880 (Electronic)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {KROL, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2006
Rederstorff M, Krol A, Lescure A
Understanding the importance of selenium and selenoproteins in muscle function Journal Article
In: Cell Mol Life Sci, vol. 63, no. 1, pp. 52-59, 2006, ISBN: 16314926, (DOI: 10.1007/s00018-005-5313-y).
Abstract | Links | BibTeX | Tags: KROL Selenium Selenoprotein Muscle disorders Congenital muscular dystrophy SEPN1, LESCURE, Unité ARN
@article{,
title = {Understanding the importance of selenium and selenoproteins in muscle function},
author = {M Rederstorff and A Krol and A Lescure},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16314926},
isbn = {16314926},
year = {2006},
date = {2006-01-01},
journal = {Cell Mol Life Sci},
volume = {63},
number = {1},
pages = {52-59},
abstract = {Selenium is an essential trace element. In cattle, selenium deficiency causes dysfunction of various organs, including skeletal and cardiac muscles. In humans as well, lack of selenium is associated with many disorders, but despite accumulation of clinical reports, muscle diseases are not generally considered on the list. The goal of this review is to establish the connection between clinical observations and the most recent advances obtained in selenium biology. Recent results about a possible role of selenium-containing proteins in muscle formation and repair have been collected. Selenoprotein N is the first selenoprotein linked to genetic disorders consisting of different forms of congenital muscular dystrophies. Understanding the muscle disorders associated with selenium deficiency or selenoprotein N dysfunction is an essential step in defining the causes of the disease and obtaining a better comprehension of the mechanisms involved in muscle formation and maintenance.},
note = {DOI: 10.1007/s00018-005-5313-y},
keywords = {KROL Selenium Selenoprotein Muscle disorders Congenital muscular dystrophy SEPN1, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Allamand V, Richard P, Lescure A, Ledeuil C, Desjardin D, Petit N, Gartioux C, Ferreiro A, Krol A, Pellegrini N, Urtizberea J A, Guicheney P
A single homozygous point mutation in a 3'untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy Journal Article
In: EMBO Rep, vol. 7, no. 4, pp. 450-454, 2006, ISBN: 16498447, (1469-221X (Print) Journal article).
Abstract | Links | BibTeX | Tags: KROL, LESCURE, Unité ARN
@article{,
title = {A single homozygous point mutation in a 3'untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy},
author = {V Allamand and P Richard and A Lescure and C Ledeuil and D Desjardin and N Petit and C Gartioux and A Ferreiro and A Krol and N Pellegrini and J A Urtizberea and P Guicheney},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16498447},
isbn = {16498447},
year = {2006},
date = {2006-01-01},
journal = {EMBO Rep},
volume = {7},
number = {4},
pages = {450-454},
abstract = {Mutations in the SEPN1 gene encoding the selenoprotein N (SelN) have been described in different congenital myopathies. Here, we report the first mutation in the selenocysteine insertion sequence (SECIS) of SelN messenger RNA, a hairpin structure located in the 3' untranslated region, in a patient presenting a classical although mild form of rigid spine muscular dystrophy. We detected a significant reduction in both mRNA and protein levels in the patient's skin fibroblasts. The SECIS element is crucial for the insertion of selenocysteine at the reprogrammed UGA codon by recruiting the SECIS-binding protein 2 (SBP2), and we demonstrated that this mutation abolishes SBP2 binding to SECIS in vitro, thereby preventing co-translational incorporation of selenocysteine and SelN synthesis. The identification of this mutation affecting a conserved base in the SECIS functional motif thereby reveals the structural basis for a novel pathological mechanism leading to SEPN1-related myopathy.},
note = {1469-221X (Print)
Journal article},
keywords = {KROL, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2005
Castellano S, Lobanov A V, Chapple C, Novoselov S V, Albrecht M, Hua D, Lescure A, Lengauer T, Krol A, Gladyshev V N, Guigo R
Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family Journal Article
In: Proc Natl Acad Sci U S A, vol. 102, no. 45, pp. 16188-16193, 2005, ISBN: 16260744, (0027-8424 (Print) Journal Article).
Abstract | Links | BibTeX | Tags: Extramural Research Support, KROL Adenosine Diphosphate Ribose/metabolism Animals Fish Proteins/chemistry/genetics/*physiology Genome Mice NIH 3T3 Cells Phylogeny Promoter Regions (Genetics) Proteome Research Support, LESCURE, N.I.H., Non-P.H.S. Selenoproteins/chemistry/genetics/*physiology Tetraodontiformes/*genetics, Non-U.S. Gov't Research Support, U.S. Gov't, Unité ARN
@article{,
title = {Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family},
author = {S Castellano and A V Lobanov and C Chapple and S V Novoselov and M Albrecht and D Hua and A Lescure and T Lengauer and A Krol and V N Gladyshev and R Guigo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16260744},
isbn = {16260744},
year = {2005},
date = {2005-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {102},
number = {45},
pages = {16188-16193},
abstract = {Selenoproteins are a diverse group of proteins that contain selenocysteine (Sec), the 21st amino acid. In the genetic code, UGA serves as a termination signal and a Sec codon. This dual role has precluded the automatic annotation of selenoproteins. Recent advances in the computational identification of selenoprotein genes have provided a first glimpse of the size, functions, and phylogenetic diversity of eukaryotic selenoproteomes. Here, we describe the identification of a selenoprotein family named SelJ. In contrast to known selenoproteins, SelJ appears to be restricted to actinopterygian fishes and sea urchin, with Cys homologues only found in cnidarians. SelJ shows significant similarity to the jellyfish J1-crystallins and with them constitutes a distinct subfamily within the large family of ADP-ribosylation enzymes. Consistent with its potential role as a structural crystallin, SelJ has preferential and homogeneous expression in the eye lens in early stages of zebrafish development. A structural role for SelJ would be in contrast to the majority of known selenoenzymes. The unusually highly restricted phylogenetic distribution of SelJ, its specialization, and the comparative analysis of eukaryotic selenoproteomes reveal the diversity and functional plasticity of selenoproteins and point to a mosaic evolution of the use of Sec in proteins.},
note = {0027-8424 (Print)
Journal Article},
keywords = {Extramural Research Support, KROL Adenosine Diphosphate Ribose/metabolism Animals Fish Proteins/chemistry/genetics/*physiology Genome Mice NIH 3T3 Cells Phylogeny Promoter Regions (Genetics) Proteome Research Support, LESCURE, N.I.H., Non-P.H.S. Selenoproteins/chemistry/genetics/*physiology Tetraodontiformes/*genetics, Non-U.S. Gov't Research Support, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2004
Jungbluth H, Beggs A, Bonnemann C, Bushby K, Groote C Ceuterick-de, Estournet-Mathiaud B, Goemans N, Guicheney P, Lescure A, Lunardi J, Muntoni F, Quinlivan R, Sewry C, Straub V, Treves S, Ferreiro A
111th ENMC International Workshop on Multi-minicore Disease. 2nd International MmD Workshop, 9-11 November 2002, Naarden, The Netherlands. Journal Article
In: Neuromuscul Disord, vol. 14, no. 11, pp. 754-766, 2004, ISBN: 15482962, (0960-8966 (Print) Congresses Research Support, Non-U.S. Gov't).
Links | BibTeX | Tags: Differential Humans Muscle Fibers/metabolism/*pathology Muscle Proteins/genetics/metabolism Muscle, KROL Diagnosis, LESCURE, Skeletal/metabolism/*pathology/physiopathology Muscular Diseases/classification/genetics/metabolism/*pathology Mutation Ryanodine Receptor Calcium Release Channel/genetics/metabolism Selenoproteins, Unité ARN
@article{,
title = {111th ENMC International Workshop on Multi-minicore Disease. 2nd International MmD Workshop, 9-11 November 2002, Naarden, The Netherlands.},
author = {H Jungbluth and A Beggs and C Bonnemann and K Bushby and C Ceuterick-de Groote and B Estournet-Mathiaud and N Goemans and P Guicheney and A Lescure and J Lunardi and F Muntoni and R Quinlivan and C Sewry and V Straub and S Treves and A Ferreiro},
url = {http://www.ncbi.nlm.nih.gov/pubmed/15482962},
isbn = {15482962},
year = {2004},
date = {2004-01-01},
journal = {Neuromuscul Disord},
volume = {14},
number = {11},
pages = {754-766},
note = {0960-8966 (Print)
Congresses
Research Support, Non-U.S. Gov't},
keywords = {Differential Humans Muscle Fibers/metabolism/*pathology Muscle Proteins/genetics/metabolism Muscle, KROL Diagnosis, LESCURE, Skeletal/metabolism/*pathology/physiopathology Muscular Diseases/classification/genetics/metabolism/*pathology Mutation Ryanodine Receptor Calcium Release Channel/genetics/metabolism Selenoproteins, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Castellano S, Novoselov S V, Kryukov G V, Lescure A, Blanco E, Krol A, Gladyshev V N, Guigo R
Reconsidering the evolution of eukaryotic selenoproteins: a novel nonmammalian family with scattered phylogenetic distribution Journal Article
In: EMBO Rep, vol. 5, no. 1, pp. 71-77, 2004, ISBN: 14710190, (1469-221x Journal Article).
Abstract | Links | BibTeX | Tags: KROL, LESCURE, Unité ARN
@article{,
title = {Reconsidering the evolution of eukaryotic selenoproteins: a novel nonmammalian family with scattered phylogenetic distribution},
author = {S Castellano and S V Novoselov and G V Kryukov and A Lescure and E Blanco and A Krol and V N Gladyshev and R Guigo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14710190},
isbn = {14710190},
year = {2004},
date = {2004-01-01},
journal = {EMBO Rep},
volume = {5},
number = {1},
pages = {71-77},
abstract = {While the genome sequence and gene content are available for an increasing number of organisms, eukaryotic selenoproteins remain poorly characterized. The dual role of the UGA codon confounds the identification of novel selenoprotein genes. Here, we describe a comparative genomics approach that relies on the genome-wide prediction of genes with in-frame TGA codons, and the subsequent comparison of predictions from different genomes, wherein conservation in regions flanking the TGA codon suggests selenocysteine coding function. Application of this method to human and fugu genomes identified a novel selenoprotein family, named SelU, in the puffer fish. The selenocysteine-containing form also occurred in other fish, chicken, sea urchin, green algae and diatoms. In contrast, mammals, worms and land plants contained cysteine homologues. We demonstrated selenium incorporation into chicken SelU and characterized the SelU expression pattern in zebrafish embryos. Our data indicate a scattered evolutionary distribution of selenoproteins in eukaryotes, and suggest that, contrary to the picture emerging from data available so far, other taxa-specific selenoproteins probably exist.},
note = {1469-221x
Journal Article},
keywords = {KROL, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2003
Thisse C, Degrave A, Kryukov G V, Gladyshev V N, Obrecht-Pflumio S, Krol A, Thisse B, Lescure A
Spatial and temporal expression patterns of selenoprotein genes during embryogenesis in zebrafish Journal Article
In: Gene Expr Patterns, vol. 3, no. 4, pp. 525-532, 2003, ISBN: 12915322, (1567-133x Journal Article).
Abstract | Links | BibTeX | Tags: Animals Gene Expression Regulation, Developmental In Situ Hybridization Molecular Sequence Data Proteins/*genetics/metabolism RNA Probes RNA, LESCURE, Messenger/metabolism Support, Non-U.S. Gov't Support, P.H.S. Tissue Distribution Zebrafish/*embryology, U.S. Gov't, Unité ARN
@article{,
title = {Spatial and temporal expression patterns of selenoprotein genes during embryogenesis in zebrafish},
author = {C Thisse and A Degrave and G V Kryukov and V N Gladyshev and S Obrecht-Pflumio and A Krol and B Thisse and A Lescure},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12915322},
isbn = {12915322},
year = {2003},
date = {2003-01-01},
journal = {Gene Expr Patterns},
volume = {3},
number = {4},
pages = {525-532},
abstract = {Selenium is important for embryogenesis in vertebrates but little is known about the expression patterns and biological functions of most selenoprotein genes. Taking advantage of the zebrafish model, systematic analysis of selenoprotein gene expression was performed by in situ hybridization on whole-mount embryos at different developmental stages. Twenty-one selenoprotein mRNAs were analyzed and all of them exhibited expression patterns restricted to specific tissues. Moreover, we demonstrated that highly similar selenoprotein paralogs were expressed within distinct territories. Therefore, tissue- and development-specific expression patterns provided new information for selenoproteins of unknown function.},
note = {1567-133x
Journal Article},
keywords = {Animals Gene Expression Regulation, Developmental In Situ Hybridization Molecular Sequence Data Proteins/*genetics/metabolism RNA Probes RNA, LESCURE, Messenger/metabolism Support, Non-U.S. Gov't Support, P.H.S. Tissue Distribution Zebrafish/*embryology, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Petit N, Lescure A, Rederstorff M, Krol A, Moghadaszadeh B, Wewer U M, Guicheney P
Selenoprotein N: an endoplasmic reticulum glycoprotein with an early developmental expression pattern Journal Article
In: Hum Mol Genet, vol. 12, no. 9, pp. 1045-1053, 2003, ISBN: 12700173, (0964-6906 Journal Article).
Abstract | Links | BibTeX | Tags: Cell Division/physiology Endoplasmic Reticulum/*metabolism Fetus/metabolism Fibroblasts/metabolism Human Muscle Proteins/*metabolism Protein Sorting Signals Support, LESCURE, Non-U.S. Gov't, Unité ARN
@article{,
title = {Selenoprotein N: an endoplasmic reticulum glycoprotein with an early developmental expression pattern},
author = {N Petit and A Lescure and M Rederstorff and A Krol and B Moghadaszadeh and U M Wewer and P Guicheney},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12700173},
isbn = {12700173},
year = {2003},
date = {2003-01-01},
journal = {Hum Mol Genet},
volume = {12},
number = {9},
pages = {1045-1053},
abstract = {Rigid spine muscular dystrophy and the classical form of multiminicore disease are caused by mutations in SEPN1 gene, leading to a new clinical entity referred to as SEPN1-related myopathy. SEPN1 codes for selenoprotein N, a new member of the selenoprotein family, the function of which is still unknown. In a previous study, two isoforms were deduced from SEPN1 transcript analyses. Using polyclonal antibodies directed against SEPN1 and cDNA constructs encoding for the two isoforms, we show that the main SEPN1 gene product corresponds to a 70 kDa protein, containing a single selenocysteine residue. Subcellular fractionation experiments and endoglycosidase H sensitivity indicate that SEPN1 is a glycoprotein-localized within the endoplasmic reticulum. Immunofluorescence analyses confirm this subcellular localization and green fluorescent protein fusion experiments demonstrate the presence of an endoplasmic reticulum-addressing and -retention signal within the N-terminus. SEPN1 is present at a high level in several human fetal tissues and at a lower level in adult ones, including skeletal muscle. Its high expression in cultured myoblasts is also down-regulated in differentiating myotubes, suggesting a role for SEPN1 in early development and in cell proliferation or regeneration.},
note = {0964-6906
Journal Article},
keywords = {Cell Division/physiology Endoplasmic Reticulum/*metabolism Fetus/metabolism Fibroblasts/metabolism Human Muscle Proteins/*metabolism Protein Sorting Signals Support, LESCURE, Non-U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2002
Lescure A, Gautheret D, Krol A
Novel selenoproteins identified from genomic sequence data Journal Article
In: Methods Enzymol, vol. 347, pp. 57-70, 2002, ISBN: 11898439, (0076-6879 Journal Article).
Links | BibTeX | Tags: 3' Untranslated Regions Animals COS Cells Codon/genetics DNA Transposable Elements DNA, Complementary/genetics Databases, Human Human Nucleic Acid Conformation Proteins/*genetics RNA, LESCURE, Messenger/chemistry/genetics Selenium Radioisotopes Support, Non-U.S. Gov't, Nucleic Acid Genome, Unité ARN
@article{,
title = {Novel selenoproteins identified from genomic sequence data},
author = {A Lescure and D Gautheret and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11898439},
isbn = {11898439},
year = {2002},
date = {2002-01-01},
journal = {Methods Enzymol},
volume = {347},
pages = {57-70},
note = {0076-6879
Journal Article},
keywords = {3' Untranslated Regions Animals COS Cells Codon/genetics DNA Transposable Elements DNA, Complementary/genetics Databases, Human Human Nucleic Acid Conformation Proteins/*genetics RNA, LESCURE, Messenger/chemistry/genetics Selenium Radioisotopes Support, Non-U.S. Gov't, Nucleic Acid Genome, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Fagegaltier D, Carbon P, Krol A
Protein factors mediating selenoprotein synthesis Journal Article
In: Curr Protein Pept Sci, vol. 3, no. 1, pp. 143-151, 2002, ISBN: 12370018, (1389-2037 Journal Article Review Review, Tutorial).
Abstract | Links | BibTeX | Tags: Bacterial Proteins/genetics/*metabolism Guanosine Triphosphate/metabolism Models, Biological Peptide Elongation Factors/*metabolism Protein Binding Proteins/*biosynthesis RNA, LESCURE, Messenger/metabolism RNA, Transfer/metabolism RNA-Binding Proteins/*metabolism, Unité ARN
@article{,
title = {Protein factors mediating selenoprotein synthesis},
author = {A Lescure and D Fagegaltier and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12370018},
isbn = {12370018},
year = {2002},
date = {2002-01-01},
journal = {Curr Protein Pept Sci},
volume = {3},
number = {1},
pages = {143-151},
abstract = {The amino acid selenocysteine represents the major biological form of selenium. Both the synthesis of selenocysteine and its co-translational incorporation into selenoproteins in response to an in-frame UGA codon, require a complex molecular machinery. To decode the UGA Sec codon in eubacteria, this machinery comprises the tRNASec, the specialized elongation factor SelB and the SECIS hairpin in the selenoprotein mRNAs. SelB conveys the Sec-tRNASec to the A site of the ribosome through binding to the SECIS mRNA hairpin adjacent to the UGA Sec codon. SelB is thus a bifunctional factor, carrying functional homology to elongation factor EF-Tu in its N-terminal domain and SECIS RNA binding activity via its C-terminal extension. In archaea and eukaryotes, selenocysteine incorporation exhibits a higher degree of complexity because the SECIS hairpin is localized in the 3' untranslated region of the mRNA. In the last couple of years, remarkable progress has been made toward understanding the underlying mechanism in mammals. Indeed, the discovery of the SECIS RNA binding protein SBP2, which is not a translation factor, paved the way for the subsequent isolation of mSelB/EFSec, the mammalian homolog of SelB. In contrast to the eubacterial SelB, the specialized elongation factor mSelB/EFSec the SECIS RNA binding function. The role is carried out by SBP2 that also forms a protein-protein complex with mSelB/EFSec. As a consequence, an important difference between the eubacterial and eukaryal selenoprotein synthesis machineries is that the functions of SelB are divided into two proteins in eukaryotes. Obviously, selenoprotein synthesis represents a higher degree of complexity than anticipated, and more needs to be discovered in eukaryotes. In this review, we will focus on the structural and functional aspects of the SelB and SBP2 factors in selenoprotein synthesis.},
note = {1389-2037
Journal Article
Review
Review, Tutorial},
keywords = {Bacterial Proteins/genetics/*metabolism Guanosine Triphosphate/metabolism Models, Biological Peptide Elongation Factors/*metabolism Protein Binding Proteins/*biosynthesis RNA, LESCURE, Messenger/metabolism RNA, Transfer/metabolism RNA-Binding Proteins/*metabolism, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Allmang C, Yamada K, Carbon P, Krol A
cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2 Journal Article
In: Gene, vol. 291, no. 1-2, pp. 279-285, 2002, ISBN: 12095701, (0378-1119 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Support, Amino Acid Sequence Blotting, Complementary/chemistry/genetics Female Gene Expression Human Male Molecular Sequence Data Peptide Elongation Factors/metabolism Protein Binding RNA/*metabolism RNA, DNA Sequence Homology, ERIANI, LESCURE, Messenger/genetics/metabolism RNA-Binding Proteins/genetics/*metabolism Sequence Alignment Sequence Analysis, Molecular DNA, Non-U.S. Gov't, Northern Cloning, Unité ARN
@article{,
title = {cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2},
author = {A Lescure and C Allmang and K Yamada and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12095701},
isbn = {12095701},
year = {2002},
date = {2002-01-01},
journal = {Gene},
volume = {291},
number = {1-2},
pages = {279-285},
abstract = {Selenocysteine and selenoprotein synthesis require a complex molecular machinery in mammals. Among the key players is the RNA-protein complex formed by the selenocysteine insertion sequence (SECIS) binding protein (SBP2) and the SECIS element, an RNA hairpin in the 3' untranslated regions of selenoprotein messenger RNAs (mRNAs). We have isolated the DNA complementary to mRNA of the human SBP2, enabling us to establish that it differs from a previously reported human SBP2-like protein. Examination of the expression pattern revealed that the human SBP2 protein is encoded by a 4 kb long mRNA that is over-expressed in testis. Compared to the rat SBP2 sequence, the human SBP2 protein displays two highly conserved domains with 92 and 95% amino acid identity, the latter one containing the RNA binding domain. The inter-domain section carries 55% sequence identity, the remainder of the SBP2 sequences showing about 65% identity, values lower than expected for two mammalian proteins. Interestingly, we could show that the binding of human SBP2 to the SECIS RNA is stimulated by the selenoprotein-specialized elongation translation factor mSelB/eEFsec.},
note = {0378-1119
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Blotting, Complementary/chemistry/genetics Female Gene Expression Human Male Molecular Sequence Data Peptide Elongation Factors/metabolism Protein Binding RNA/*metabolism RNA, DNA Sequence Homology, ERIANI, LESCURE, Messenger/genetics/metabolism RNA-Binding Proteins/genetics/*metabolism Sequence Alignment Sequence Analysis, Molecular DNA, Non-U.S. Gov't, Northern Cloning, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lambert A, Lescure A, Gautheret D
A survey of metazoan selenocysteine insertion sequences Journal Article
In: Biochimie, vol. 84, no. 9, pp. 953-959, 2002, ISBN: 12458087, (0300-9084 Journal Article).
Abstract | Links | BibTeX | Tags: Animals Base Sequence *Conserved Sequence Databases, Genetic Human Molecular Sequence Data Nucleic Acid Conformation Proteins/*genetics Selenocysteine/*genetics/metabolism Sequence Alignment Sequence Homology, LESCURE, Nucleic Acid Software, Unité ARN
@article{,
title = {A survey of metazoan selenocysteine insertion sequences},
author = {A Lambert and A Lescure and D Gautheret},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12458087},
isbn = {12458087},
year = {2002},
date = {2002-01-01},
journal = {Biochimie},
volume = {84},
number = {9},
pages = {953-959},
abstract = {The computational detection of novel selenoproteins in genomic sequences is usually achieved through identification of SECIS, a conserved secondary structure element found in the 3' UTR of animal selenoprotein mRNAs. Previous studies have used "descriptors" specifying the number of base pairs and the conserved nucleotides in SECIS to identify this element. A major drawback of the "descriptor" approach is that the number of detections in current genomic or transcript databases largely exceeds the number of true selenoproteins. In this study, we use instead the ERPIN program to detect SECIS elements. ERPIN is based on a lod-score profile algorithm that uses a training-set of aligned RNA sequences as input. From an initial alignment of 44 animal SECIS sequences, we performed a series of iterative searches in which the training set was progressively enriched up to 117 confirmed SECIS elements, from a large collection of metazoan species. About 200 high-scoring candidates were also detected. We show that ERPIN scores for these candidates can be converted into expect values, thus enabling their statistical evaluation. The most interesting SECIS candidates are presented.},
note = {0300-9084
Journal Article},
keywords = {Animals Base Sequence *Conserved Sequence Databases, Genetic Human Molecular Sequence Data Nucleic Acid Conformation Proteins/*genetics Selenocysteine/*genetics/metabolism Sequence Alignment Sequence Homology, LESCURE, Nucleic Acid Software, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2000
Libri D, Lescure A, Rosbash M
Splicing enhancement in the yeast rp51b intron Journal Article
In: RNA, vol. 6, no. 3, pp. 352-368, 2000, ISBN: 10744020, (1355-8382 Journal Article).
Abstract | Links | BibTeX | Tags: 5' Untranslated Regions/genetics DNA Mutational Analysis Introns/*genetics Multigene Family Nucleic Acid Conformation RNA Splicing/*genetics *Regulatory Sequences, LESCURE, Non-U.S. Gov't Support, Nucleic Acid Ribonucleoprotein, P.H.S. Uridine/metabolism, U.S. Gov't, U1 Small Nuclear/chemistry/genetics Saccharomyces cerevisiae/*genetics Support, Unité ARN
@article{,
title = {Splicing enhancement in the yeast rp51b intron},
author = {D Libri and A Lescure and M Rosbash},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10744020},
isbn = {10744020},
year = {2000},
date = {2000-01-01},
journal = {RNA},
volume = {6},
number = {3},
pages = {352-368},
abstract = {Splicing enhancement in higher eukaryotes has been linked to SR proteins, to U1 snRNP, and to communication between splice sites across introns or exons mediated by protein-protein interactions. It has been previously shown that, in yeast, communication mediated by RNA-RNA interactions between the two ends of introns is a basis for splicing enhancement. We designed experiments of randomization-selection to isolate splicing enhancers that would work independently from RNA secondary structures. Surprisingly, one of the two families of sequences selected was essentially composed of 5' splice site variants. We show that this sequence enhances splicing independently of secondary structure, is exportable to heterologous contexts, and works in multiple copies with additive effects. The data argue in favor of an early role for splicing enhancement, possibly coincident with commitment complex formation. Genetic compensation experiments with U1 snRNA mutants suggest that U1 snRNP binding to noncanonical locations is required for splicing enhancement.},
note = {1355-8382
Journal Article},
keywords = {5' Untranslated Regions/genetics DNA Mutational Analysis Introns/*genetics Multigene Family Nucleic Acid Conformation RNA Splicing/*genetics *Regulatory Sequences, LESCURE, Non-U.S. Gov't Support, Nucleic Acid Ribonucleoprotein, P.H.S. Uridine/metabolism, U.S. Gov't, U1 Small Nuclear/chemistry/genetics Saccharomyces cerevisiae/*genetics Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Gautheret D, Fagegaltier D, Carbon P, Krol A
From RNA structure to the identification of new genes: the example of selenoproteins Journal Article
In: J Health Sci, vol. 46, no. 6, pp. 405-408, 2000, ISBN: 01A0078173.
Links | BibTeX | Tags: KROL ACL, LESCURE, Unité ARN
@article{,
title = {From RNA structure to the identification of new genes: the example of selenoproteins},
author = {A Lescure and D Gautheret and D Fagegaltier and P Carbon and A Krol},
url = {http://sciencelinks.jp/j-east/article/200107/000020010701A0078173.php},
isbn = {01A0078173},
year = {2000},
date = {2000-01-01},
journal = {J Health Sci},
volume = {46},
number = {6},
pages = {405-408},
keywords = {KROL ACL, LESCURE, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Fagegaltier D, Lescure A, Walczak R, Carbon P, Krol A
Structural analysis of new local features in SECIS RNA hairpins Journal Article
In: Nucleic Acids Res, vol. 28, no. 14, pp. 2679-2689, 2000, ISBN: 10908323, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Animals Base Sequence COS Cells DNA/chemistry/genetics DNA, DNA Support, Factual Drosophila melanogaster/genetics Glutathione Peroxidase/genetics/metabolism Human Mice Molecular Sequence Data Mutagenesis, LESCURE, Non-U.S. Gov't Xenopus laevis, Nucleic Acid/*genetics Selenocysteine/*genetics/metabolism Sequence Alignment Sequence Analysis, Recombinant/genetics/metabolism Databases, Site-Directed Nucleic Acid Conformation Phosphotransferases/genetics RNA/chemistry/*genetics Rats Regulatory Sequences, Unité ARN
@article{,
title = {Structural analysis of new local features in SECIS RNA hairpins},
author = {D Fagegaltier and A Lescure and R Walczak and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10908323},
isbn = {10908323},
year = {2000},
date = {2000-01-01},
journal = {Nucleic Acids Res},
volume = {28},
number = {14},
pages = {2679-2689},
abstract = {Decoding of the UGA selenocysteine codon for selenoprotein translation requires the SECIS element, a stem-loop motif in the 3'-UTR of the mRNA carrying short or large apical loops. In previous structural studies, we derived a secondary structure model for SECIS RNAs with short apical loops. Work from others proposed that intra-apical loop base pairing can occur in those SECIS that possess large apical loops, yielding form 2 SECIS versus the form 1 with short loops. In this work, SECIS elements arising from eight different selenoprotein mRNAs were assayed by enzymatic and/or chemical probing showing that seven can adopt form 2. Further, database searches led to the discovery in drosophila and zebrafish of SECIS elements in the selenophosphate synthetase 2, type 1 deiodinase and SelW mRNAs. Alignment of SECIS sequences not only highlighted the predominance of form 2 but also made it possible to classify the SECIS elements according to the type of selenoprotein mRNA they belong to. Interestingly, the alignment revealed that an unpaired adenine, previously thought to be invariant, is replaced by a guanine in four SECIS elements. Tested in vivo, neither the A to G nor the A to U changes at this position greatly affected the activity while the most detrimental effect was provided by a C. The putative contribution of the various SECIS motifs to function and ligand binding is discussed.},
note = {1362-4962
Journal Article},
keywords = {Animals Base Sequence COS Cells DNA/chemistry/genetics DNA, DNA Support, Factual Drosophila melanogaster/genetics Glutathione Peroxidase/genetics/metabolism Human Mice Molecular Sequence Data Mutagenesis, LESCURE, Non-U.S. Gov't Xenopus laevis, Nucleic Acid/*genetics Selenocysteine/*genetics/metabolism Sequence Alignment Sequence Analysis, Recombinant/genetics/metabolism Databases, Site-Directed Nucleic Acid Conformation Phosphotransferases/genetics RNA/chemistry/*genetics Rats Regulatory Sequences, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1994
Sturchler C, Lescure A, Keith G, Carbon P, Krol A
Base modification pattern at the wobble position of Xenopus selenocysteine tRNA(Sec) Journal Article
In: Nucleic Acids Res, vol. 22, no. 8, pp. 1354-1358, 1994, ISBN: 8031393, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid-Specific/chemistry/*genetics/metabolism Selenocysteine/*metabolism Support, Animals *Anticodon Base Composition Base Sequence Microinjections Molecular Sequence Data Mutagenesis Nucleic Acid Conformation RNA, LESCURE, Non-U.S. Gov't Uridine Xenopus laevis, Transfer, Unité ARN
@article{,
title = {Base modification pattern at the wobble position of Xenopus selenocysteine tRNA(Sec)},
author = {C Sturchler and A Lescure and G Keith and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8031393},
isbn = {8031393},
year = {1994},
date = {1994-01-01},
journal = {Nucleic Acids Res},
volume = {22},
number = {8},
pages = {1354-1358},
abstract = {We examined the base modification pattern of Xenopus tRNA(Sec) using microinjection into Xenopus oocytes, with particular focus on the wobble base U34 at the first position of the anticodon. We found that U34 becomes modified to mcm5U34 (5-methylcarboxymethyluridine) in the oocyte cytoplasm in a rather complex manner. When the tRNA(Sec) gene is injected into Xenopus oocyte nuclei, psi 55 and m1A58 are readily obtained, but not mcm5U34. This will appear only upon cytoplasmic injection of the gene product arising from the first nuclear injection. In contrast, tRNA(Sec) produced by in vitro transcription with T7 RNA polymerase readily acquires i6A37, psi 55, m1A58, and mcm5U34. The latter is obtained after direct nuclear or cytoplasmic injections. It has been reported by others that mcm5Um, a 2'-O-methylated derivative of mcm5U34, also exists in rat and bovine tRNA(Sec). With both the gene product and the in vitro transcript, and using the sensitive RNase T2 assay, we were unable to detect under our conditions the presence of a dinucleotide carrying mcm5Um and that would be therefore refractory to hydrolysis. We showed that the unusual mcm5U acquisition pathway does not result from impairment of nucleocytoplasmic transport. Rather, these data can be interpreted to mean that the modification is performed by a tRNA(Sec) specific enzyme, limiting in the oocyte cytoplasm.},
note = {0305-1048
Journal Article},
keywords = {Amino Acid-Specific/chemistry/*genetics/metabolism Selenocysteine/*metabolism Support, Animals *Anticodon Base Composition Base Sequence Microinjections Molecular Sequence Data Mutagenesis Nucleic Acid Conformation RNA, LESCURE, Non-U.S. Gov't Uridine Xenopus laevis, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Lutz Y, Eberhard D, Jacq X, Krol A, Grummt I, Davidson I, Chambon P, Tora L
The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters Journal Article
In: EMBO J, vol. 13, no. 5, pp. 1166-1175, 1994, ISBN: 7510635, (0261-4189 Journal Article).
Abstract | Links | BibTeX | Tags: Antibodies, Genetic, LESCURE, Non-U.S. Gov't *TATA Box TATA-Box Binding Protein Transcription Factor TFIIA Transcription Factor TFIIB Transcription Factor TFIID Transcription Factors/biosynthesis/isolation & purification/*metabolism *Transcription, Unité ARN
@article{,
title = {The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters},
author = {A Lescure and Y Lutz and D Eberhard and X Jacq and A Krol and I Grummt and I Davidson and P Chambon and L Tora},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7510635},
isbn = {7510635},
year = {1994},
date = {1994-01-01},
journal = {EMBO J},
volume = {13},
number = {5},
pages = {1166-1175},
abstract = {In eukaryotes, the TATA box binding protein (TBP) is an integral component of the transcription initiation complexes of all three classes of nuclear RNA polymerases. In this study we have investigated the role of the N-terminal region of human TBP in transcription initiation from RNA polymerase (Pol) I, II and III promoters by using three monoclonal antibodies (mAbs). Each antibody recognizes a distinct epitope in the N-terminal domain of human TBP. We demonstrate that these antibodies differentially affect transcription from distinct classes of promoters. One antibody, mAb1C2, and a synthetic peptide comprising its epitope selectively inhibited in vitro transcription from TATA-containing, but not from TATA-less promoters, irrespective of whether they were transcribed by Pol II or Pol III. Transcription by Pol I, on the other hand, was not affected. Two other antibodies and their respective epitope peptides did not affect transcription from any of the promoters tested. Order of addition experiments indicate that mAb1C2 did not prevent binding of TBP to the TATA box or the formation of the TBP-TFIIA-TFIIB complex but rather inhibited a subsequent step of preinitiation complex formation. These data suggest that a defined region within the N-terminal domain of human TBP may be involved in specific protein-protein interactions required for the assembly of functional preinitiation complexes on TATA-containing, but not on TATA-less promoters.},
note = {0261-4189
Journal Article},
keywords = {Antibodies, Genetic, LESCURE, Non-U.S. Gov't *TATA Box TATA-Box Binding Protein Transcription Factor TFIIA Transcription Factor TFIIB Transcription Factor TFIID Transcription Factors/biosynthesis/isolation & purification/*metabolism *Transcription, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1992
Lescure A, Tebb G, Mattaj I W, Krol A, Carbon P
A factor with Sp1 DNA-binding specificity stimulates Xenopus U6 snRNA in vivo transcription by RNA polymerase III Journal Article
In: J Mol Biol, vol. 228, no. 2, pp. 387-394, 1992, ISBN: 1453450, (0022-2836 Journal Article).
Abstract | Links | BibTeX | Tags: Animals Base Sequence Binding Sites Dna Molecular Sequence Data RNA Polymerase III/*metabolism RNA, Genetic Xenopus, LESCURE, Non-U.S. Gov't Transcription Factor, Nucleic Acid Support, Small Nuclear/*genetics *Regulatory Sequences, Sp1/metabolism *Transcription, Unité ARN
@article{,
title = {A factor with Sp1 DNA-binding specificity stimulates Xenopus U6 snRNA in vivo transcription by RNA polymerase III},
author = {A Lescure and G Tebb and I W Mattaj and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1453450},
isbn = {1453450},
year = {1992},
date = {1992-01-01},
journal = {J Mol Biol},
volume = {228},
number = {2},
pages = {387-394},
abstract = {We have previously shown that transcription of the Xenopus U6 snRNA gene by RNA polymerase III is stimulated in injected Xenopus oocytes by an activator element termed the DSE, which contains an octamer sequence. Data presented here reveal that the DSE contains, in addition, a GC-rich sequence capable of binding Sp1. Both elements are required to obtain wild-type levels of U6 transcription in vivo. The Xenopus U6 DSE exhibits optimal activation properties only when positioned at its normal location upstream from the start site. The U6 Sp1 motif binds the mammalian Sp1 transcriptional activator independently of the Oct-1 protein in vitro. Those mutations that lead to a reduced transcription level in vivo abolish the binding of Sp1 in vitro. Thus, transcriptional stimulation through the Xenopus U6 Sp1 motif is likely to be mediated by a protein with DNA-binding specificity identical to mammalian Sp1. These findings support the notion that RNA polymerase II and III transcription complexes share transactivators.},
note = {0022-2836
Journal Article},
keywords = {Animals Base Sequence Binding Sites Dna Molecular Sequence Data RNA Polymerase III/*metabolism RNA, Genetic Xenopus, LESCURE, Non-U.S. Gov't Transcription Factor, Nucleic Acid Support, Small Nuclear/*genetics *Regulatory Sequences, Sp1/metabolism *Transcription, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Murgo S, Carbon P, Krol A
The proximal promoter and the start site cooperate to specify correct U1 snRNA transcription initiation by RNA polymerase II Journal Article
In: Nucleic Acids Res, vol. 20, no. 7, pp. 1573-1578, 1992, ISBN: 1579449, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Animals Base Sequence DNA/metabolism DNA Mutational Analysis Molecular Sequence Data Promoter Regions (Genetics)/*genetics RNA Polymerase II/*metabolism RNA, Genetic/*genetics Xenopus laevis/genetics, KROL, LESCURE, Non-U.S. Gov't Transcription, Small Nuclear/*genetics Support, Unité ARN
@article{,
title = {The proximal promoter and the start site cooperate to specify correct U1 snRNA transcription initiation by RNA polymerase II},
author = {A Lescure and S Murgo and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1579449},
isbn = {1579449},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {7},
pages = {1573-1578},
abstract = {In this work, we attempted to gain insight into the detailed mechanism allowing correct transcription initiation of U1 snRNA genes by RNA polymerase II. Abolition of the CA motif residing at -1/+1 in the Xenopus U1 gene leads to a loss of the ability of the promoter to direct accurate initiation. A discrete site is selected only if a purine preceded by a pyrimidine is positioned at 58/57 bp downstream of the center of the PSE. The PSE alone is unable to designate a discrete initiation site. Rather, it serves to set the location of an initiation window without discriminating suitable from unsuitable initiation sites. The latter role is devoted to a PyPu sequence positioned at -1/+1. Therefore, it is the concomitant action of the PSE and an essential PyPu positioned at the proper distance from this promoter that specifies correct U1 snRNA transcription initiation by RNA polymerase II.},
note = {0305-1048
Journal Article},
keywords = {Animals Base Sequence DNA/metabolism DNA Mutational Analysis Molecular Sequence Data Promoter Regions (Genetics)/*genetics RNA Polymerase II/*metabolism RNA, Genetic/*genetics Xenopus laevis/genetics, KROL, LESCURE, Non-U.S. Gov't Transcription, Small Nuclear/*genetics Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}