Publications
2023
Wright Duncan E, Krol Alain
FEBS fellowships: supporting excellent science for over four decades Divers
2023, ISSN: 2211-5463.
Résumé | Liens | BibTeX | Étiquettes: KROL, Unité ARN
@misc{pmid37394995,
title = {FEBS fellowships: supporting excellent science for over four decades},
author = {Duncan E Wright and Alain Krol},
doi = {10.1002/2211-5463.13659},
issn = {2211-5463},
year = {2023},
date = {2023-07-01},
urldate = {2023-07-01},
journal = {FEBS Open Bio},
volume = {13},
number = {7},
pages = {1138--1139},
abstract = {The Federation of European Biochemical Societies (FEBS) awarded FEBS Long-Term Fellowships from 1979 until 2020, at which time the scheme was replaced with the FEBS Excellence Award. Over four decades, FEBS awarded a huge number of Long-Term Fellowships, helping to support and promote the careers of excellent young researchers across Europe. To celebrate the exciting work performed by the FEBS Long-Term Fellows, we present here a special 'In the Limelight' issue of FEBS Open Bio, containing four Mini-reviews and four Research Protocols authored by the fellows themselves. The four Review articles provide timely updates on the respective research fields, while the Research Protocols describe how to perform challenging experimental methods in detail. We hope this issue will be a valuable resource for the community, and a celebration of the high-quality work done by young scientists.},
keywords = {KROL, Unité ARN},
pubstate = {published},
tppubtype = {misc}
}
2012
Lescure A, Castets P, Grunwald D, Allamand V, Howard M
Selenoprotein N: Its role in disease. Chapitre d'ouvrage
Dans: Hatfield, D; Berry, M; Gladyshev, V (Ed.): Selenium: Its molecular biology and role in human health, p. 283-294, Springer, 2, 2012.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
Allmang C, Krol A
Seleneoprotein biosynthesis Chapitre d'ouvrage
Dans: Liu, J; Luo, G; Mu, Y (Ed.): Selenoproteins and Mimics, p. 107-124, Springer, 2012.
Résumé | Liens | BibTeX | Étiquettes: ERIANI, KROL, Unité ARN
@inbook{,
title = {Seleneoprotein biosynthesis},
author = {C Allmang and A Krol},
editor = {J Liu and G Luo and Y Mu},
url = {http://www.springerlink.com/content/q4h42729317k1478/},
doi = {10.1007/978-3-642-22236-8_8},
year = {2012},
date = {2012-01-01},
booktitle = {Selenoproteins and Mimics},
pages = {107-124},
publisher = {Springer},
series = {Advanced Topics and Technology in China},
abstract = {The amino acid selenocysteine (Sec) is the major biological form of the trace element selenium. Sec is co-translationally incorporated in selenoproteins and is found in the active site of those that have already been assigned a function. In eukaryotes, Sec biosynthesis from serine on the selenocysteine transfer RNA (tRNASec) requires four enzymes. The synthesis of selenoproteins follows a remarkable mechanism which involves translational recoding of a UGA codon, normally used as a stop signal, into a Sec codon. A surprisingly high number of molecular partners have been identified in this machinery but their mechanism of action is still largely unknown. In this chapter, we will provide a detailed description of the knowledge of the field.},
keywords = {ERIANI, KROL, Unité ARN},
pubstate = {published},
tppubtype = {inbook}
}
2011
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. Article de journal
Dans: PLoS One, vol. 6, no. 8, p. e23094, 2011, ISBN: 21858002.
Résumé | Liens | BibTeX | Étiquettes: 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
Takeuchi A, Schmitt D, Chapple C, Babaylova E, Karpova G, Guigo R, Krol A, Allmang C
A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins Article de journal
Dans: Nucleic Acids Res, vol. 37, no. 7, p. 2126-2141, 2009, ISBN: 19223320, (1362-4962 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: ERIANI, KROL, Unité ARN
@article{,
title = {A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins},
author = {A Takeuchi and D Schmitt and C Chapple and E Babaylova and G Karpova and R Guigo and A Krol and C Allmang},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19223320},
isbn = {19223320},
year = {2009},
date = {2009-01-01},
journal = {Nucleic Acids Res},
volume = {37},
number = {7},
pages = {2126-2141},
abstract = {Selenoproteins contain the amino acid selenocysteine which is encoded by a UGA Sec codon. Recoding UGA Sec requires a complex mechanism, comprising the cis-acting SECIS RNA hairpin in the 3'UTR of selenoprotein mRNAs, and trans-acting factors. Among these, the SECIS Binding Protein 2 (SBP2) is central to the mechanism. SBP2 has been so far functionally characterized only in rats and humans. In this work, we report the characterization of the Drosophila melanogaster SBP2 (dSBP2). Despite its shorter length, it retained the same selenoprotein synthesis-promoting capabilities as the mammalian counterpart. However, a major difference resides in the SECIS recognition pattern: while human SBP2 (hSBP2) binds the distinct form 1 and 2 SECIS RNAs with similar affinities, dSBP2 exhibits high affinity toward form 2 only. In addition, we report the identification of a K (lysine)-rich domain in all SBP2s, essential for SECIS and 60S ribosomal subunit binding, differing from the well-characterized L7Ae RNA-binding domain. Swapping only five amino acids between dSBP2 and hSBP2 in the K-rich domain conferred reversed SECIS-binding properties to the proteins, thus unveiling an important sequence for form 1 binding.},
note = {1362-4962 (Electronic)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {ERIANI, KROL, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Hirosawa-Takamori M, Ossipov D, Novoselov S V, Turanov A A, Zhang Y, Gladyshev V N, Krol A, Vorbruggen G, Jackle H
A novel stem loop control element-dependent UGA read-through system without translational selenocysteine incorporation in Drosophila Article de journal
Dans: Faseb J, vol. 23, no. 1, p. 107-113, 2009, ISBN: 18772345, (1530-6860 (Electronic) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: KROL, Unité ARN
@article{,
title = {A novel stem loop control element-dependent UGA read-through system without translational selenocysteine incorporation in Drosophila},
author = {M Hirosawa-Takamori and D Ossipov and S V Novoselov and A A Turanov and Y Zhang and V N Gladyshev and A Krol and G Vorbruggen and H Jackle},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18772345},
isbn = {18772345},
year = {2009},
date = {2009-01-01},
journal = {Faseb J},
volume = {23},
number = {1},
pages = {107-113},
abstract = {Translational read-through of the UGA stop codon is an evolutionarily conserved feature that most prominently represents the basis of selenoprotein biosynthesis. It requires a specific cis-acting stem loop control element, termed SECIS, which is located in the 3'-untranslated region of eukaryotic selenoprotein mRNAs. In a search for novel factors underlying the SECIS-directed UGA read-through process, we identified an evolutionary conserved GTPase-activating protein, termed GAPsec. We show that the activity of the Drosophila GAPsec (dGAPsec) is necessary to support SECIS-dependent UGA read-through activity in flies and the mouse homolog mGAPsec in mice tissue culture cells. However, selenoprotein biosynthesis is not impaired in flies that lack dGAPsec activity. The results indicate that GAPsec is part of a novel SECIS-dependent translational read-through system that does not involve selenocysteine incorporation.},
note = {1530-6860 (Electronic)
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't},
keywords = {KROL, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Chapple C E, Guigo R, Krol A
SECISaln, a web-based tool for the creation of structure-based alignments of eukaryotic SECIS elements Article de journal
Dans: Bioinformatics, vol. 25, no. 5, p. 674-675, 2009, ISBN: 19179357, (1460-2059 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: KROL, Unité ARN
@article{,
title = {SECISaln, a web-based tool for the creation of structure-based alignments of eukaryotic SECIS elements},
author = {C E Chapple and R Guigo and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19179357},
isbn = {19179357},
year = {2009},
date = {2009-01-01},
journal = {Bioinformatics},
volume = {25},
number = {5},
pages = {674-675},
abstract = {SUMMARY: Selenoproteins contain the 21st amino acid selenocysteine which is encoded by an inframe UGA codon, usually read as a stop. In eukaryotes, its co-translational recoding requires the presence of an RNA stem-loop structure, the SECIS element in the 3 untranslated region of (UTR) selenoprotein mRNAs. Despite little sequence conservation, SECIS elements share the same overall secondary structure. Until recently, the lack of a significantly high number of selenoprotein mRNA sequences hampered the identification of other potential sequence conservation. In this work, the web-based tool SECISaln provides for the first time an extensive structure-based sequence alignment of SECIS elements resulting from the well-defined secondary structure of the SECIS RNA and the increased size of the eukaryotic selenoproteome. We have used SECISaln to improve our knowledge of SECIS secondary structure and to discover novel, conserved nucleotide positions and we believe it will be a useful tool for the selenoprotein and RNA scientific communities. AVAILABILITY: SECISaln is freely available as a web-based tool at http://genome.crg.es/software/secisaln/.},
note = {1460-2059 (Electronic)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {KROL, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2008
Geary C., Baudrey S., Jaeger L.
Comprehensive features of natural and in vitro selected GNRA tetraloop-binding receptors Article de journal
Dans: Nucleic Acids Res, vol. 36, no. 4, p. 1138-52, 2008, (1362-4962 (Electronic) Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.).
Résumé | BibTeX | Étiquettes: Acid, Adenine/chemistry, Analysis, Base, Conformation, Data, dimerization, directed, Evolution, KROL, Models, Molecular, Nucleic, RNA, RNA/*chemistry/classification, Sequence, Thermodynamics
@article{,
title = {Comprehensive features of natural and in vitro selected GNRA tetraloop-binding receptors},
author = { C. Geary and S. Baudrey and L. Jaeger},
year = {2008},
date = {2008-01-01},
journal = {Nucleic Acids Res},
volume = {36},
number = {4},
pages = {1138-52},
abstract = {Specific recognitions of GNRA tetraloops by small helical receptors are among the most widespread long-range packing interactions in large ribozymes. However, in contrast to GYRA and GAAA tetraloops, very few GNRA/receptor interactions have yet been identified to involve GGAA tetraloops in nature. A novel in vitro selection scheme based on a rigid self-assembling tectoRNA scaffold designed for isolation of intermolecular interactions with A-minor motifs has yielded new GGAA tetraloop-binding receptors with affinity in the nanomolar range. One of the selected receptors is a novel 12 nt RNA motif, (CCUGUG. AUCUGG), that recognizes GGAA tetraloop hairpin with a remarkable specificity and affinity. Its physical and chemical characteristics are comparable to those of the well-studied '11nt' GAAA tetraloop receptor motif. A second less specific motif (CCCAGCCC. GAUAGGG) binds GGRA tetraloops and appears to be related to group IC3 tetraloop receptors. Mutational, thermodynamic and comparative structural analysis suggests that natural and in vitro selected GNRA receptors can essentially be grouped in two major classes of GNRA binders. New insights about the evolution, recognition and structural modularity of GNRA and A-minor RNA-RNA interactions are proposed.},
note = {1362-4962 (Electronic)
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.},
keywords = {Acid, Adenine/chemistry, Analysis, Base, Conformation, Data, dimerization, directed, Evolution, KROL, Models, Molecular, Nucleic, RNA, RNA/*chemistry/classification, Sequence, Thermodynamics},
pubstate = {published},
tppubtype = {article}
}
Lescure A, Deniziak M, Rederstorff M, Krol A
Molecular basis for the role of selenium in muscle development and function Article de journal
Dans: Chem Biodivers, vol. 5, no. 3, p. 408-413, 2008, ISBN: 18357550, (1612-1880 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Liens | BibTeX | Étiquettes: 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
Myslinski E, Gerard M A, Krol A, Carbon P
A genome scale location analysis of human Staf/ZNF143-binding sites suggests a widespread role for human Staf/ZNF143 in mammalian promoters Article de journal
Dans: J Biol Chem, vol. 281, no. 52, p. 39953-39962, 2006, ISBN: 17092945, (0021-9258 (Print) Journal Article).
Résumé | Liens | BibTeX | Étiquettes: KROL, Unité ARN
@article{,
title = {A genome scale location analysis of human Staf/ZNF143-binding sites suggests a widespread role for human Staf/ZNF143 in mammalian promoters},
author = {E Myslinski and M A Gerard and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17092945},
isbn = {17092945},
year = {2006},
date = {2006-01-01},
journal = {J Biol Chem},
volume = {281},
number = {52},
pages = {39953-39962},
abstract = {Staf was originally identified as the transcriptional activator of Xenopus tRNA(Sec) and small nuclear (sn) RNA-type genes. Recently, transcription of seven human (h) protein coding genes was reported to be activated by the human ortholog hStaf/ZNF143. Here we have used a combined in silico and biochemical approach to identify 1175 conserved hStaf/ZNF143-binding sites (SBS) distributed in 938 promoters of four mammalian genomes. The SBS shows a significant positional preference and occurs mostly within 200 bp upstream of the transcription start site. Chromatin immunoprecipitation assays with 295 of the promoters established that 90% contain bona fide SBS. By extrapolating the values of this mapping to the full sizes of the mammalian genomes, we can infer the existence of at least 2500 SBS distributed in 2000 promoters. This unexpected large number strongly suggests that SBS constitutes one of the most widespread transcription factor-binding sites in mammalian promoters. Furthermore, we demonstrated that the presence of the SBS alone is sufficient to direct expression of a luciferase reporter gene, suggesting that hStaf/ZNF143 can recruit per se the transcription machinery.},
note = {0021-9258 (Print)
Journal Article},
keywords = {KROL, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Allmang C, Krol A
Selenoprotein synthesis: UGA does not end the story Article de journal
Dans: Biochimie, vol. 88, no. 11, p. 1561-1571, 2006, ISBN: 16737768, (0300-9084 (Print) Journal Article).
Résumé | Liens | BibTeX | Étiquettes: KROL, Unité ARN
@article{,
title = {Selenoprotein synthesis: UGA does not end the story},
author = {C Allmang and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16737768},
isbn = {16737768},
year = {2006},
date = {2006-01-01},
journal = {Biochimie},
volume = {88},
number = {11},
pages = {1561-1571},
abstract = {It is well established that the beneficial effects of the trace element selenium are mediated by its major biological product, the amino acid selenocysteine, present in the active site of selenoproteins. These fulfill different functions, as varied as oxidation-reduction of metabolites in bacteria, reduction of reactive oxygen species, control of the redox status of the cell or thyroid hormone maturation. This review will focus on the singularities of the selenocysteine biosynthesis pathway and its unique incorporation mechanism into eukaryal selenoproteins. Selenocysteine biosynthesis from serine is achieved on tRNA(Sec) and requires four proteins. As this amino acid is encoded by an in-frame UGA codon, otherwise signaling termination of translation, ribosomes must be told not to stop at this position in the mRNA. Several molecular partners acting in cis or in trans have been identified, but their knowledge has not enabled yet to firmly establish the molecular events underlying this mechanism. Data suggest that other, so far uncharacterized factors might exist. In this survey, we attempted to compile all the data available in the literature and to describe the latest developments in the field.},
note = {0300-9084 (Print)
Journal Article},
keywords = {KROL, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Allmang C, Krol A
SECIS RNAs and K-turn binding proteins. A survey of evolutionary conserved RNA and protein motifs. Chapitre d'ouvrage
Dans: Hatfield, D L; Berry, M J; Gladyshev, V N (Ed.): Selenium, Its Molecular Biology and Role in Human Health, p. 51-61, Springer US, 2006, ISBN: 10.1007/0-387-33827-6_5.
Résumé | Liens | BibTeX | Étiquettes: KROL, Unité ARN
@inbook{,
title = {SECIS RNAs and K-turn binding proteins. A survey of evolutionary conserved RNA and protein motifs.},
author = {C Allmang and A Krol},
editor = {D L Hatfield and M J Berry and V N Gladyshev},
url = {http://www.springerlink.com/content/m854145547561671},
isbn = {10.1007/0-387-33827-6_5},
year = {2006},
date = {2006-01-01},
booktitle = {Selenium, Its Molecular Biology and Role in Human Health},
pages = {51-61},
publisher = {Springer US},
abstract = {The SelenoCysteine Insertion Sequence (SECIS) is a stem-loop structure residing in the 3? untranslated region of all selenoprotein mRNAs. Its presence is mandatory to allow the ribosome to readthrough the UGA selenocysteine codon. The SECIS RNA possesses a well-defined secondary structure. Four consecutive non-Watson-Crick base pairs, with a central tandem of sheared G.A/A.G base pairs, constitute the functional motif of the SECIS RNA which is recognized by the SECIS binding protein SBP2. The tandem of sheared base pairs is part of a recurrent motif, the kink-turn (K-turn), occurring in a variety of different RNAs. The K-turn is a helix-internal loop-helix composed of a non-Watson-Crick stem containing the G.A base pairs and a canonical stem. The internal loop between the stems is always asymmetrical and usually contains three unpaired nucleotides on one strand and none on the other. We propose here that the SECIS RNA must represent a K-turn variant with regard to the limited structural differences that distinguish it from consensus K-turns. Work by others showed that ribosomal protein L30 also binds the SECIS RNA in a specific manner. L30 and SBP2 are members of a family of proteins sharing the same RNA-binding domain called L7A/L30. All proteins possessing this fold recognize K-turn RNAs. Three structures of RNA-protein complexes containing the L7A/L30 protein fold and cognate K-turn RNAs have been solved. In light of the interaction principles governing these RNA-protein complexes, we discuss how L30 can recognize the SECIS RNA. Collectively, all the findings suggest that the L7A/L30 protein fold and the K-turn are ancient structural motifs that have evolved various functions, from pre-mRNA splicing to protein synthesis.},
keywords = {KROL, Unité ARN},
pubstate = {published},
tppubtype = {inbook}
}
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 Article de journal
Dans: EMBO Rep, vol. 7, no. 4, p. 450-454, 2006, ISBN: 16498447, (1469-221X (Print) Journal article).
Résumé | Liens | BibTeX | Étiquettes: 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}
}
2004
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 Article de journal
Dans: EMBO Rep, vol. 5, no. 1, p. 71-77, 2004, ISBN: 14710190, (1469-221x Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 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}
}
1992
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 Article de journal
Dans: Nucleic Acids Res, vol. 20, no. 7, p. 1573-1578, 1992, ISBN: 1579449, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 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}
}