Zhang H, Kolb F A, Jaskiewicz L, Westhof E, Filipowicz W
Single processing center models for human Dicer and bacterial RNase III Article de journal
Dans: Cell, vol. 118, no. 1, p. 57-68, 2004, ISBN: 15242644, (0092-8674 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Support, Amino Acid Sequence Base Sequence Comparative Study Conserved Sequence Dimerization Endoribonucleases/*chemistry/genetics/isolation & purification/*metabolism Escherichia coli/enzymology Human Manganese/metabolism MicroRNAs/metabolism Models, Double-Stranded/chemistry/*metabolism RNA, Molecular Molecular Sequence Data Molecular Weight Mutagenesis, Non-U.S. Gov't, Post-Transcriptional RNA, Secondary Protein Structure, Site-Directed Mutation Protein Structure, Small Interfering/metabolism Recombinant Proteins/metabolism Ribonuclease III/*chemistry/genetics/isolation & purification/*metabolism Sequence Homology, Tertiary RNA Helicases/*chemistry/genetics/isolation & purification/*metabolism *RNA Processing, Unité ARN, WESTHOF
@article{,
title = {Single processing center models for human Dicer and bacterial RNase III},
author = {H Zhang and F A Kolb and L Jaskiewicz and E Westhof and W Filipowicz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15242644},
isbn = {15242644},
year = {2004},
date = {2004-01-01},
journal = {Cell},
volume = {118},
number = {1},
pages = {57-68},
abstract = {Dicer is a multidomain ribonuclease that processes double-stranded RNAs (dsRNAs) to 21 nt small interfering RNAs (siRNAs) during RNA interference, and excises microRNAs from precursor hairpins. Dicer contains two domains related to the bacterial dsRNA-specific endonuclease, RNase III, which is known to function as a homodimer. Based on an X-ray structure of the Aquifex aeolicus RNase III, models of the enzyme interaction with dsRNA, and its cleavage at two composite catalytic centers, have been proposed. We have generated mutations in human Dicer and Escherichia coli RNase III residues implicated in the catalysis, and studied their effect on RNA processing. Our results indicate that both enzymes have only one processing center, containing two RNA cleavage sites and generating products with 2 nt 3' overhangs. Based on these and other data, we propose that Dicer functions through intramolecular dimerization of its two RNase III domains, assisted by the flanking RNA binding domains, PAZ and dsRBD.},
note = {0092-8674
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Base Sequence Comparative Study Conserved Sequence Dimerization Endoribonucleases/*chemistry/genetics/isolation & purification/*metabolism Escherichia coli/enzymology Human Manganese/metabolism MicroRNAs/metabolism Models, Double-Stranded/chemistry/*metabolism RNA, Molecular Molecular Sequence Data Molecular Weight Mutagenesis, Non-U.S. Gov't, Post-Transcriptional RNA, Secondary Protein Structure, Site-Directed Mutation Protein Structure, Small Interfering/metabolism Recombinant Proteins/metabolism Ribonuclease III/*chemistry/genetics/isolation & purification/*metabolism Sequence Homology, Tertiary RNA Helicases/*chemistry/genetics/isolation & purification/*metabolism *RNA Processing, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}
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}
}
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}
}
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}
}
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}
}