Publications
2005
Ryckelynck M, Masquida B, Giege R, Frugier M
An intricate RNA structure with two tRNA-derived motifs directs complex formation between yeast aspartyl-tRNA synthetase and its mRNA Article de journal
Dans: J Mol Biol, vol. 354, no. 3, p. 614-629, 2005, ISBN: 16257416, (0022-2836 (Print) Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Aspartate-tRNA Ligase/genetics/*metabolism Base Sequence DNA Footprinting Gene Deletion Models, FRUGIER, Messenger/*chemistry/*metabolism RNA, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Structure, Non-U.S. Gov't Saccharomyces cerevisiae/*enzymology/*genetics Sequence Alignment Sequence Homology, Nucleic Acid Solubility, Tertiary RNA, Transfer/*chemistry/*metabolism Research Support, Unité ARN
@article{,
title = {An intricate RNA structure with two tRNA-derived motifs directs complex formation between yeast aspartyl-tRNA synthetase and its mRNA},
author = {M Ryckelynck and B Masquida and R Giege and M Frugier},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16257416},
isbn = {16257416},
year = {2005},
date = {2005-01-01},
journal = {J Mol Biol},
volume = {354},
number = {3},
pages = {614-629},
abstract = {Accurate translation of genetic information necessitates the tuned expression of a large group of genes. Amongst them, controlled expression of the enzymes catalyzing the aminoacylation of tRNAs, the aminoacyl-tRNA synthetases, is essential to insure translational fidelity. In the yeast Saccharomyces cerevisiae, expression of aspartyl-tRNA synthetase (AspRS) is regulated in a process necessitating recognition of the 5' extremity of AspRS messenger RNA (mRNA(AspRS)) by its translation product and adaptation to the cellular tRNA(Asp) concentration. Here, we have established the folding of the approximately 300 nucleotides long 5' end of mRNA(AspRS) and identified the structural signals involved in the regulation process. We show that the regulatory region in mRNA(AspRS) folds in two independent and symmetrically structured domains spaced by two single-stranded connectors. Domain I displays a tRNA(Asp) anticodon-like stem-loop structure with mimics of the aspartate identity determinants, that is restricted in domain II to a short double-stranded helix. The overall mRNA structure, based on enzymatic and chemical probing, supports a three-dimensional model where each monomer of yeast AspRS binds one individual domain and recognizes the mRNA structure as it recognizes its cognate tRNA(Asp). Sequence comparison of yeast genomes shows that the features within the mRNA recognized by AspRS are conserved in different Saccharomyces species. In the recognition process, the N-terminal extension of each AspRS subunit plays a crucial role in anchoring the tRNA-like motifs of the mRNA on the synthetase.},
note = {0022-2836 (Print)
Journal Article},
keywords = {Aspartate-tRNA Ligase/genetics/*metabolism Base Sequence DNA Footprinting Gene Deletion Models, FRUGIER, Messenger/*chemistry/*metabolism RNA, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Structure, Non-U.S. Gov't Saccharomyces cerevisiae/*enzymology/*genetics Sequence Alignment Sequence Homology, Nucleic Acid Solubility, Tertiary RNA, Transfer/*chemistry/*metabolism Research Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Graindorge J S, Senger B, Tritch D, Simos G, Fasiolo F
Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity Article de journal
Dans: Biochemistry, vol. 44, no. 4, p. 1344-1352, 2005, ISBN: 15667228, (0006-2960 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: FASIOLO Adenosine Triphosphate/chemistry/metabolism Amino Acid Sequence Aminoacylation Base Sequence Diphosphates/chemistry/metabolism Enzyme Activation Gene Expression Regulation, Fungal Glutamate-tRNA Ligase/isolation & purification/*metabolism Kinetics Molecular Sequence Data Peptide Fragments/chemistry/metabolism Protein Binding Protein Structure, Fungal/genetics/metabolism RNA, Genetic, Glu/genetics/metabolism RNA-Binding Proteins/*chemistry/isolation & purification/metabolism Research Support, Non-U.S. Gov't Saccharomyces cerevisiae/enzymology/genetics/metabolism Saccharomyces cerevisiae Proteins/*chemistry/isolation & purification/metabolism Transcription, Tertiary RNA, Transfer, Unité ARN
@article{,
title = {Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity},
author = {J S Graindorge and B Senger and D Tritch and G Simos and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15667228},
isbn = {15667228},
year = {2005},
date = {2005-01-01},
journal = {Biochemistry},
volume = {44},
number = {4},
pages = {1344-1352},
abstract = {Yeast methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS) possess N-terminal extensions that bind the cofactor Arc1p in trans. The strength of GluRS-Arc1p interaction is high enough to allow copurification of the two macromolecules in a 1:1 ratio, in contrast to MetRS. Deletion analysis from the C-terminal end of the GluRS appendix combined with previous N-terminal deletions of GluRS allows restriction of the Arc1p binding site to the 110-170 amino acid region of GluRS. This region has been shown to correspond to a novel protein-protein interaction domain present in both GluRS and Arc1p but not in MetRS [Galani, K., Grosshans, H., Deinert, K., Hurt, E. C., and Simos, G. (2001) EMBO J. 20, 6889-6898]. The GluRS apoenzyme fails to show significant kinetics of tRNA aminoacylation and charges unfractionated yeast tRNA at a level 10-fold reduced compared to Arc1p-bound GluRS. The K(m) values for tRNA(Glu) measured in the ATP-PP(i) exchange were similar for the two forms of GluRS, whereas k(cat) is increased 2-fold in the presence of Arc1p. Band-shift analysis revealed a 100-fold increase in tRNA binding affinity when Arc1p is bound to GluRS. This increase requires the RNA binding properties of the full-length Arc1p since Arc1p N domain leaves the K(d) of GluRS for tRNA unchanged. Transcripts of yeast tRNA(Glu) were poor substrates for measuring tRNA aminoacylation and could not be used to clarify whether Arc1p has a specific effect on the tRNA charging reaction.},
note = {0006-2960
Journal Article},
keywords = {FASIOLO Adenosine Triphosphate/chemistry/metabolism Amino Acid Sequence Aminoacylation Base Sequence Diphosphates/chemistry/metabolism Enzyme Activation Gene Expression Regulation, Fungal Glutamate-tRNA Ligase/isolation & purification/*metabolism Kinetics Molecular Sequence Data Peptide Fragments/chemistry/metabolism Protein Binding Protein Structure, Fungal/genetics/metabolism RNA, Genetic, Glu/genetics/metabolism RNA-Binding Proteins/*chemistry/isolation & purification/metabolism Research Support, Non-U.S. Gov't Saccharomyces cerevisiae/enzymology/genetics/metabolism Saccharomyces cerevisiae Proteins/*chemistry/isolation & purification/metabolism Transcription, Tertiary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2004
Martin F, Barends S, Eriani G
Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo Article de journal
Dans: Nucleic Acids Res, vol. 32, no. 13, p. 4081-4089, 2004, ISBN: 15289581, (1362-4962 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Substitution Anticodon/metabolism Aspartate-tRNA Ligase/*chemistry/genetics/*metabolism Aspartic Acid/metabolism Binding Sites Models, Amino Acyl/chemistry/*metabolism Support, ERIANI, Molecular Mutation Phenotype Protein Engineering Protein Structure, Non-U.S. Gov't, Tertiary RNA, Transfer, Unité ARN
@article{,
title = {Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo},
author = {F Martin and S Barends and G Eriani},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15289581},
isbn = {15289581},
year = {2004},
date = {2004-01-01},
journal = {Nucleic Acids Res},
volume = {32},
number = {13},
pages = {4081-4089},
abstract = {Aminoacyl-tRNA synthetases (aaRSs) are enzymes that are highly specific for their tRNA substrates. Here, we describe the expansion of a class IIb aaRS-tRNA specificity by a genetic selection that involves the use of a modified tRNA displaying an amber anticodon and the argE(amber) and lacZ(amber) reporters. The study was performed on Escherichia coli aspartyl-tRNA synthetase (AspRS) and amber tRNA(Asp). Nine AspRS mutants able to charge the amber tRNA(Asp) and to suppress the reporter genes were selected from a randomly mutated library. All the mutants exhibited a new amber tRNA(Asp) specificity in addition to the initial native tRNA(Asp). Six mutations were found in the anticodon-binding site located in the N-terminal OB-fold. The strongest suppressor was a mutation of residue Glu-93 that contacts specifically the anticodon nucleotide 34 in the crystal structure. The other mutations in the OB-fold were found at close distance from the anticodon in the so-called loop L45 and strand S1. They concern residues that do not contact tRNA(Asp) in the native complex. In addition, this study shows that suppressors can carry mutations located far from the anticodon-binding site. One such mutation was found in the synthetase hinge-module where it increases the tRNA(Asp)-charging rate, and two other mutations were found in the prokaryotic-specific insertion domain and the catalytic core. These mutants seem to act by indirect effects on the tRNA acceptor stem binding and on the conformation of the active site of the enzyme. Altogether, these data suggest the existence of various ways for modifying the mechanism of tRNA discrimination.},
note = {1362-4962
Journal Article},
keywords = {Amino Acid Substitution Anticodon/metabolism Aspartate-tRNA Ligase/*chemistry/genetics/*metabolism Aspartic Acid/metabolism Binding Sites Models, Amino Acyl/chemistry/*metabolism Support, ERIANI, Molecular Mutation Phenotype Protein Engineering Protein Structure, Non-U.S. Gov't, Tertiary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Dubois D Y, Blaise M, Becker H D, Campanacci V, Keith G, Giege R, Cambillau C, Lapointe J, Kern D
An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 101, no. 20, p. 7530-7535, 2004, ISBN: 15096594, (0027-8424 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/*metabolism Support, KERN GIEGE Amino Acyl-tRNA Ligases/chemistry/genetics/*metabolism Crystallography, Messenger/metabolism RNA, Non-U.S. Gov't, Tertiary RNA, Transfer, Unité ARN, X-Ray Escherichia coli/enzymology/genetics/*metabolism Escherichia coli Proteins/chemistry/genetics/*metabolism Glutamic Acid/*metabolism Peptide Elongation Factor 2/metabolism Phylogeny Protein Structure
@article{,
title = {An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp},
author = {D Y Dubois and M Blaise and H D Becker and V Campanacci and G Keith and R Giege and C Cambillau and J Lapointe and D Kern},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15096594},
isbn = {15096594},
year = {2004},
date = {2004-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {101},
number = {20},
pages = {7530-7535},
abstract = {The product of the Escherichia coli yadB gene is homologous to the N-terminal part of bacterial glutamyl-tRNA synthetases (GluRSs), including the Rossmann fold with the acceptor-binding domain and the stem-contact fold. This GluRS-like protein, which lacks the anticodon-binding domain, does not use tRNA(Glu) as substrate in vitro nor in vivo, but aminoacylates tRNA(Asp) with glutamate. The yadB gene is expressed in wild-type E. coli as an operon with the dksA gene, which encodes a protein involved in the general stress response by means of its action at the translational level. The fate of the glutamylated tRNA(Asp) is not known, but its incapacity to bind elongation factor Tu suggests that it is not involved in ribosomal protein synthesis. Genes homologous to yadB are present only in bacteria, mostly in Proteobacteria. Sequence alignments and phylogenetic analyses show that the YadB proteins form a distinct monophyletic group related to the bacterial and organellar GluRSs (alpha-type GlxRSs superfamily) with ubiquitous function as suggested by the similar functional properties of the YadB homologue from Neisseria meningitidis.},
note = {0027-8424
Journal Article},
keywords = {Asp/*metabolism Support, KERN GIEGE Amino Acyl-tRNA Ligases/chemistry/genetics/*metabolism Crystallography, Messenger/metabolism RNA, Non-U.S. Gov't, Tertiary RNA, Transfer, Unité ARN, X-Ray Escherichia coli/enzymology/genetics/*metabolism Escherichia coli Proteins/chemistry/genetics/*metabolism Glutamic Acid/*metabolism Peptide Elongation Factor 2/metabolism Phylogeny Protein Structure},
pubstate = {published},
tppubtype = {article}
}
2003
Ryckelynck M, Giege R, Frugier M
Yeast tRNA(Asp) charging accuracy is threatened by the N-terminal extension of aspartyl-tRNA synthetase Article de journal
Dans: J Biol Chem, vol. 278, no. 11, p. 9683-9690, 2003, ISBN: 12486031, (0021-9258 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Motifs Aspartate-tRNA Ligase/*metabolism Aspartic Acid/chemistry Base Sequence Codon Escherichia coli/metabolism Kinetics Molecular Sequence Data Nucleic Acid Conformation Nucleic Acids/chemistry Protein Structure, Asp/*chemistry Support, FRUGIER, Messenger/metabolism RNA, Non-U.S. Gov't Yeasts/metabolism, Secondary Protein Structure, Tertiary RNA, Transfer, Unité ARN
@article{,
title = {Yeast tRNA(Asp) charging accuracy is threatened by the N-terminal extension of aspartyl-tRNA synthetase},
author = {M Ryckelynck and R Giege and M Frugier},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12486031},
isbn = {12486031},
year = {2003},
date = {2003-01-01},
journal = {J Biol Chem},
volume = {278},
number = {11},
pages = {9683-9690},
abstract = {This study evaluates the role of the N-terminal extension from yeast aspartyl-tRNA synthetase in tRNA aspartylation. The presence of an RNA-binding motif in this extension, conserved in eukaryotic class IIb aminoacyl-tRNA synthetases, provides nonspecific tRNA binding properties to this enzyme. Here, it is assumed that the additional contacts the 70 amino acid-long appendix of aspartyl-tRNA synthetase makes with tRNA could be important in expression of aspartate identity in yeast. Using in vitro transcripts mutated at identity positions, it is demonstrated that the extension grants better aminoacylation efficiency but reduced specificity to the synthetase, increasing considerably the risk of noncognate tRNA mischarging. Yeast tRNA(Glu(UUC)) and tRNA(Asn(GUU)) were identified as the most easily mischarged tRNA species. Both have a G at the discriminator position, and their anticodon differs only by one change from the GUC aspartate anticodon.},
note = {0021-9258
Journal Article},
keywords = {Amino Acid Motifs Aspartate-tRNA Ligase/*metabolism Aspartic Acid/chemistry Base Sequence Codon Escherichia coli/metabolism Kinetics Molecular Sequence Data Nucleic Acid Conformation Nucleic Acids/chemistry Protein Structure, Asp/*chemistry Support, FRUGIER, Messenger/metabolism RNA, Non-U.S. Gov't Yeasts/metabolism, Secondary Protein Structure, Tertiary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Rangan P, Masquida B, Westhof E, Woodson S A
Assembly of core helices and rapid tertiary folding of a small bacterial group I ribozyme Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 100, no. 4, p. 1574-1579, 2003, ISBN: 12574513, (0027-8424 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Azoarcus/*enzymology Base Sequence Introns Magnesium/chemistry Models, Catalytic/*chemistry/genetics Support, Molecular Molecular Sequence Data Nucleic Acid Conformation *Protein Folding Protein Structure, Non-U.S. Gov't Support, P.H.S., Tertiary RNA, U.S. Gov't, Unité ARN, WESTHOF
@article{,
title = {Assembly of core helices and rapid tertiary folding of a small bacterial group I ribozyme},
author = {P Rangan and B Masquida and E Westhof and S A Woodson},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12574513},
isbn = {12574513},
year = {2003},
date = {2003-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {100},
number = {4},
pages = {1574-1579},
abstract = {Compact but non-native intermediates have been implicated in the hierarchical folding of several large RNAs, but there is little information on their structure. In this article, ribonuclease and hydroxyl radical cleavage protection assays showed that base pairing of core helices stabilize a compact state of a small group I ribozyme from Azoarcus pre-tRNA(ile). Base pairing of the ribozyme core requires 10-fold less Mg(2+) than stable tertiary interactions, indicating that assembly of helices in the catalytic core represents a distinct phase that precedes the formation of native tertiary structure. Tertiary folding occurs in <100 ms at 37 degrees C. Such rapid folding is unprecedented among group I ribozymes and illustrates the association between structural complexity and folding time. A 3D model of the Azoarcus ribozyme was constructed by identifying homologous sequence motifs in rRNA. The model reveals distinct structural features, such as a large interface between the P4-P6 and P3-P9 domains, that may explain the unusual stability of the Azoarcus ribozyme and the cooperativity of folding.},
note = {0027-8424
Journal Article},
keywords = {Azoarcus/*enzymology Base Sequence Introns Magnesium/chemistry Models, Catalytic/*chemistry/genetics Support, Molecular Molecular Sequence Data Nucleic Acid Conformation *Protein Folding Protein Structure, Non-U.S. Gov't Support, P.H.S., Tertiary RNA, U.S. Gov't, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}
2002
Vicens Q, Westhof E
Crystal structure of a complex between the aminoglycoside tobramycin and an oligonucleotide containing the ribosomal decoding a site Article de journal
Dans: Chem Biol, vol. 9, no. 6, p. 747-755, 2002, ISBN: 12079787, (1074-5521 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 16S/*chemistry Support, Anti-Bacterial Agents/*chemistry Binding Sites Crystallography Escherichia coli/metabolism Models, Molecular Oligonucleotides/*chemistry Paromomycin/chemistry Protein Structure, Non-U.S. Gov't Tobramycin/*chemistry, Ribosomal, Secondary Protein Structure, Tertiary RNA, Unité ARN, WESTHOF
@article{,
title = {Crystal structure of a complex between the aminoglycoside tobramycin and an oligonucleotide containing the ribosomal decoding a site},
author = {Q Vicens and E Westhof},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12079787},
isbn = {12079787},
year = {2002},
date = {2002-01-01},
journal = {Chem Biol},
volume = {9},
number = {6},
pages = {747-755},
abstract = {Aminoglycoside antibiotics target the decoding aminoacyl site (A site) on the 16S ribosomal RNA and induce miscoding during translation. Here, we present the crystal structure, at 2.54 A resolution, of an RNA oligonucleotide containing the A site sequence complexed to the 4,6-disubstituted 2-deoxystreptamine aminoglycoside tobramycin. The three aminosugar rings making up tobramycin interact with the deep-groove atoms directly or via water molecules and stabilize a fully bulged-out conformation of adenines A(1492) and A(1493). The comparison between this structure and the one previously solved in the presence of paromomycin confirms the importance of the functional groups on the common neamine part of these two antibiotics for binding to RNA. Furthermore, the analysis of the present structure provides a molecular explanation to some of the resistance mechanisms that have spread among bacteria and rendered aminoglycoside antibiotics inefficient.},
note = {1074-5521
Journal Article},
keywords = {16S/*chemistry Support, Anti-Bacterial Agents/*chemistry Binding Sites Crystallography Escherichia coli/metabolism Models, Molecular Oligonucleotides/*chemistry Paromomycin/chemistry Protein Structure, Non-U.S. Gov't Tobramycin/*chemistry, Ribosomal, Secondary Protein Structure, Tertiary RNA, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}
Serganov A, Ennifar E, Portier C, Ehresmann B, Ehresmann C
Do mRNA and rRNA binding sites of E.coli ribosomal protein S15 share common structural determinants? Article de journal
Dans: J Mol Biol, vol. 320, no. 5, p. 963-978, 2002, ISBN: 12126618, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Binding Sites Cytosine Escherichia coli Guanosine Models, ENNIFAR, Messenger/*chemistry RNA, Molecular Nucleic Acid Conformation Protein Structure, Non-U.S. Gov't Uridine, Ribosomal/*chemistry Ribosomal Proteins/*chemistry Support, Tertiary RNA, Unité ARN
@article{,
title = {Do mRNA and rRNA binding sites of E.coli ribosomal protein S15 share common structural determinants?},
author = {A Serganov and E Ennifar and C Portier and B Ehresmann and C Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12126618},
isbn = {12126618},
year = {2002},
date = {2002-01-01},
journal = {J Mol Biol},
volume = {320},
number = {5},
pages = {963-978},
abstract = {Escherichia coli ribosomal protein S15 recognizes two RNA targets: a three-way junction in 16S rRNA and a pseudoknot structure on its own mRNA. Binding to mRNA occurs when S15 is expressed in excess over its rRNA target, resulting in an inhibition of translation start. The sole apparent similarity between the rRNA and mRNA targets is the presence of a G-U/G-C motif that contributes only modestly to rRNA binding but is essential for mRNA. To get more information on the structural determinants used by S15 to bind its mRNA target as compared to its rRNA site, we used site-directed mutagenesis, substitution by nucleotide analogs, footprinting experiments on both RNA and protein, and graphic modeling. The size of the mRNA-binding site could be reduced to 45 nucleotides, without loss of affinity. This short RNA preferentially folds into a pseudoknot, the formation of which depends on magnesium concentration and temperature. The size of the loop L2 that bridges the two stems of the pseudoknot through the minor groove could not be reduced below nine nucleotides. Then we showed that the pseudoknot recognizes the same side of S15 as 16S rRNA, although shielding a smaller surface area. It turned out that the G-U/G-C motif is recognized from the minor groove in both cases, and that the G-C pair is recognized in a very similar manner. However, the wobble G-U pair of the mRNA is not directly contacted by S15, as in rRNA, but is most likely involved in building a precise conformation of the RNA, essential for binding. Otherwise, unique specific features are utilized, such as the three-way junction in the case of 16S rRNA and the looped out A(-46) for the mRNA pseudoknot.},
note = {0022-2836
Journal Article},
keywords = {Binding Sites Cytosine Escherichia coli Guanosine Models, ENNIFAR, Messenger/*chemistry RNA, Molecular Nucleic Acid Conformation Protein Structure, Non-U.S. Gov't Uridine, Ribosomal/*chemistry Ribosomal Proteins/*chemistry Support, Tertiary RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1999
Sankaranarayanan R, Dock-Bregeon A C, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D
The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site Article de journal
Dans: Cell, vol. 97, no. 3, p. 371-381, 1999, ISBN: 10319817, (0092-8674 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Support, Amino Acyl/*chemistry/genetics/*metabolism Sequence Homology, Messenger/genetics RNA, Non-U.S. Gov't Zinc/*chemistry, ROMBY, Secondary Protein Structure, Tertiary RNA, Transfer, Unité ARN
@article{,
title = {The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site},
author = {R Sankaranarayanan and A C Dock-Bregeon and P Romby and J Caillet and M Springer and B Rees and C Ehresmann and B Ehresmann and D Moras},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10319817},
isbn = {10319817},
year = {1999},
date = {1999-01-01},
journal = {Cell},
volume = {97},
number = {3},
pages = {371-381},
abstract = {E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that represses the translation of its own mRNA. We report the crystal structure at 2.9 A resolution of the complex between tRNA(Thr) and ThrRS, whose structural features reveal novel strategies for providing specificity in tRNA selection. These include an amino-terminal domain containing a novel protein fold that makes minor groove contacts with the tRNA acceptor stem. The enzyme induces a large deformation of the anticodon loop, resulting in an interaction between two adjacent anticodon bases, which accounts for their prominent role in tRNA identity and translational regulation. A zinc ion found in the active site is implicated in amino acid recognition/discrimination.},
note = {0092-8674
Journal Article},
keywords = {Amino Acid Support, Amino Acyl/*chemistry/genetics/*metabolism Sequence Homology, Messenger/genetics RNA, Non-U.S. Gov't Zinc/*chemistry, ROMBY, Secondary Protein Structure, Tertiary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1996
Senger B, Fasiolo F
Yeast tRNA(Met) recognition by methionyl-tRNA synthetase requires determinants from the primary, secondary and tertiary structure: a review Article de journal
Dans: Biochimie, vol. 78, no. 7, p. 597-604, 1996, ISBN: 8955903, (0300-9084 Journal Article Review Review, Tutorial).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence Anticodon Methionine-tRNA Ligase/*metabolism Molecular Sequence Data Nucleic Acid Conformation Protein Structure, Met/*metabolism Structure-Activity Relationship Support, Non-U.S. Gov't, Secondary Protein Structure, Tertiary RNA, Transfer, Unité ARN
@article{,
title = {Yeast tRNA(Met) recognition by methionyl-tRNA synthetase requires determinants from the primary, secondary and tertiary structure: a review},
author = {B Senger and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8955903},
isbn = {8955903},
year = {1996},
date = {1996-01-01},
journal = {Biochimie},
volume = {78},
number = {7},
pages = {597-604},
abstract = {The primordial role of the CAU anticodon in methionine identity of the tRNA has been established by others nearly a decade ago in Escherichia coli and yeast tRNA(Met). We show here that the CAU triplet alone is unable to confer methionine acceptance to a tRNA. This requires the contribution of the discriminatory base A73 and the non-anticodon bases of the anticodon loop. To better understand the functional communication between the anticodon and the active site, we analysed the binding and aminoacylation of tRNA(Met) based anticodon and acceptor-stem minihelices and of tRNA(Met) chimeras where the central core region of yeast tRNA(Met) is replaced by that of unusual mitochondrial forms lacking either a D-stem or a T-stem. These studies suggest that the high selectivity of the anticodon bases in tRNA(Met) implies the L-conformation of the tRNA and the presence of a D-stem. The importance of a L-structure for recognition of tRNA(Met) was also deduced from mutations of tertiary interactions known to play a general role in tRNA(Met) folding.},
note = {0300-9084
Journal Article
Review
Review, Tutorial},
keywords = {Amino Acid Sequence Anticodon Methionine-tRNA Ligase/*metabolism Molecular Sequence Data Nucleic Acid Conformation Protein Structure, Met/*metabolism Structure-Activity Relationship Support, Non-U.S. Gov't, Secondary Protein Structure, Tertiary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}