Blaise M, Becker H D, Keith G, Cambillau C, Lapointe J, Giege R, Kern D
A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon Article de journal
Dans: Nucleic Acids Res, vol. 32, no. 9, p. 2768-2775, 2004, ISBN: 15150343, (1362-4962 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/chemistry/genetics/*metabolism RNA, Bacterial/chemistry/genetics/metabolism RNA, Glu/chemistry/genetics/metabolism Support, KERN Acylation Anticodon/chemistry/genetics/*metabolism Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics Evolution Glutamate-tRNA Ligase/*chemistry/genetics/*metabolism Molecular Mimicry Nucleoside Q/genetics/*metabolism Periodic Acid/pharmacology RNA, Non-U.S. Gov't, Transfer, Unité ARN
@article{,
title = {A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon},
author = {M Blaise and H D Becker and G Keith and C Cambillau and J Lapointe and R Giege and D Kern},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15150343},
isbn = {15150343},
year = {2004},
date = {2004-01-01},
journal = {Nucleic Acids Res},
volume = {32},
number = {9},
pages = {2768-2775},
abstract = {Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl-tRNA synthetase but lacking the anticodon-binding domain. We show that YadB is a tRNA modifying enzyme that evidently glutamylates the queuosine residue, a modified nucleoside at the wobble position of the tRNA(Asp) QUC anticodon. This conclusion is supported by a variety of biochemical data and by the inability of the enzyme to glutamylate tRNA(Asp) isolated from an E.coli tRNA-guanosine transglycosylase minus strain deprived of the capacity to exchange guanosine 34 with queuosine. Structural mimicry between the tRNA(Asp) anticodon stem and the tRNA(Glu) amino acid acceptor stem in prokaryotes encoding YadB proteins indicates that the function of these tRNA modifying enzymes, which we rename glutamyl-Q tRNA(Asp) synthetases, is conserved among prokaryotes.},
note = {1362-4962
Journal Article},
keywords = {Asp/chemistry/genetics/*metabolism RNA, Bacterial/chemistry/genetics/metabolism RNA, Glu/chemistry/genetics/metabolism Support, KERN Acylation Anticodon/chemistry/genetics/*metabolism Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics Evolution Glutamate-tRNA Ligase/*chemistry/genetics/*metabolism Molecular Mimicry Nucleoside Q/genetics/*metabolism Periodic Acid/pharmacology RNA, Non-U.S. Gov't, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Tsai H Y, Masquida B, Biswas R, Westhof E, Gopalan V
Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme Article de journal
Dans: J Mol Biol, vol. 325, no. 4, p. 661-675, 2003, ISBN: 12507471, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence Base Sequence Catalytic Domain Computer Simulation Cysteine/chemistry DNA Footprinting DNA, Bacterial/chemistry/genetics/metabolism RNA, Bacterial/genetics Edetic Acid Endoribonucleases/*chemistry/genetics/metabolism Escherichia coli/*enzymology/genetics Evolution, Catalytic/*chemistry/genetics/metabolism Ribonuclease P Support, Molecular Ferrous Compounds Holoenzymes/chemistry/genetics/metabolism Hydroxyl Radical/chemistry Models, Molecular Molecular Sequence Data Mutagenesis, Non-P.H.S. Support, P.H.S., Site-Directed Nucleic Acid Conformation Protein Subunits RNA, U.S. Gov't, Unité ARN, WESTHOF
@article{,
title = {Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme},
author = {H Y Tsai and B Masquida and R Biswas and E Westhof and V Gopalan},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12507471},
isbn = {12507471},
year = {2003},
date = {2003-01-01},
journal = {J Mol Biol},
volume = {325},
number = {4},
pages = {661-675},
abstract = {Bacterial ribonuclease P (RNase P), an enzyme involved in tRNA maturation, consists of a catalytic RNA subunit and a protein cofactor. Comparative phylogenetic analysis and molecular modeling have been employed to derive secondary and tertiary structure models of the RNA subunits from Escherichia coli (type A) and Bacillus subtilis (type B) RNase P. The tertiary structure of the protein subunit of B.subtilis and Staphylococcus aureus RNase P has recently been determined. However, an understanding of the structure of the RNase P holoenzyme (i.e. the ribonucleoprotein complex) is lacking. We have now used an EDTA-Fe-based footprinting approach to generate information about RNA-protein contact sites in E.coli RNase P. The footprinting data, together with results from other biochemical and biophysical studies, have furnished distance constraints, which in turn have enabled us to build three-dimensional models of both type A and B versions of the bacterial RNase P holoenzyme in the absence and presence of its precursor tRNA substrate. These models are consistent with results from previous studies and provide both structural and mechanistic insights into the functioning of this unique catalytic RNP complex.},
note = {0022-2836
Journal Article},
keywords = {Amino Acid Sequence Base Sequence Catalytic Domain Computer Simulation Cysteine/chemistry DNA Footprinting DNA, Bacterial/chemistry/genetics/metabolism RNA, Bacterial/genetics Edetic Acid Endoribonucleases/*chemistry/genetics/metabolism Escherichia coli/*enzymology/genetics Evolution, Catalytic/*chemistry/genetics/metabolism Ribonuclease P Support, Molecular Ferrous Compounds Holoenzymes/chemistry/genetics/metabolism Hydroxyl Radical/chemistry Models, Molecular Molecular Sequence Data Mutagenesis, Non-P.H.S. Support, P.H.S., Site-Directed Nucleic Acid Conformation Protein Subunits RNA, U.S. Gov't, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}
Torres-Larios A, Dock-Bregeon A C, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D
Structural basis of translational control by Escherichia coli threonyl tRNA synthetase Article de journal
Dans: Nat Struct Biol, vol. 9, no. 5, p. 343-347, 2002, ISBN: 11953757, (1072-8368 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon/genetics Base Sequence Crystallography, Bacterial/chemistry/genetics/metabolism RNA, Genetic, Messenger/chemistry/genetics/*metabolism RNA, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Conformation RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*chemistry/*metabolism *Translation, ROMBY, Transfer/chemistry/genetics/metabolism Sequence Alignment Structure-Activity Relationship Support, Unité ARN, X-Ray Escherichia coli/*enzymology/genetics Models
@article{,
title = {Structural basis of translational control by Escherichia coli threonyl tRNA synthetase},
author = {A Torres-Larios and A C Dock-Bregeon and P Romby and B Rees and R Sankaranarayanan and J Caillet and M Springer 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=11953757},
isbn = {11953757},
year = {2002},
date = {2002-01-01},
journal = {Nat Struct Biol},
volume = {9},
number = {5},
pages = {343-347},
abstract = {Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to the enzyme surface. The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-negative bacteria.},
note = {1072-8368
Journal Article},
keywords = {Anticodon/genetics Base Sequence Crystallography, Bacterial/chemistry/genetics/metabolism RNA, Genetic, Messenger/chemistry/genetics/*metabolism RNA, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Conformation RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*chemistry/*metabolism *Translation, ROMBY, Transfer/chemistry/genetics/metabolism Sequence Alignment Structure-Activity Relationship Support, Unité ARN, X-Ray Escherichia coli/*enzymology/genetics Models},
pubstate = {published},
tppubtype = {article}
}
Nikulin A, Serganov A, Ennifar E, Tishchenko S, Nevskaya N, Shepard W, Portier C, Garber M, Ehresmann B, Ehresmann C, Nikonov S, Dumas P
Crystal structure of the S15-rRNA complex Article de journal
Dans: Nat Struct Biol, vol. 7, no. 4, p. 273-277, 2000, ISBN: 10742169, (1072-8368 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 16S/*chemistry/genetics/*metabolism Ribosomal Proteins/*chemistry/*metabolism Structure-Activity Relationship Support, Amino Acid Sequence Base Pairing/drug effects/genetics Base Sequence Binding Sites/drug effects Conserved Sequence/genetics Crystallography, Bacterial/chemistry/genetics/metabolism RNA, ENNIFAR, Molecular Molecular Sequence Data *Nucleic Acid Conformation/drug effects Protein Conformation RNA, Non-U.S. Gov't Thermus thermophilus/*chemistry/genetics, Ribosomal, Unité ARN, X-Ray Magnesium/pharmacology Models
@article{,
title = {Crystal structure of the S15-rRNA complex},
author = {A Nikulin and A Serganov and E Ennifar and S Tishchenko and N Nevskaya and W Shepard and C Portier and M Garber and B Ehresmann and C Ehresmann and S Nikonov and P Dumas},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10742169},
isbn = {10742169},
year = {2000},
date = {2000-01-01},
journal = {Nat Struct Biol},
volume = {7},
number = {4},
pages = {273-277},
abstract = {In bacterial ribosomes, the small (30S) ribosomal subunit is composed of 16S rRNA and 21 distinct proteins. Ribosomal protein S15 is of particular interest because it binds primarily to 16S rRNA and is required for assembly of the small subunit and for intersubunit association, thus representing a key element in the assembly of a whole ribosome. Here we report the 2.8 inverted question mark resolution crystal structure of the highly conserved S15-rRNA complex. Protein S15 interacts in the minor groove with a G-U/G-C motif and a three-way junction. The latter is constrained by a conserved base triple and stacking interactions, and locked into place by magnesium ions and protein side chains, mainly through interactions with the unique three-dimensional geometry of the backbone. The present structure gives insights into the dual role of S15 in ribosome assembly and translational regulation.},
note = {1072-8368
Journal Article},
keywords = {16S/*chemistry/genetics/*metabolism Ribosomal Proteins/*chemistry/*metabolism Structure-Activity Relationship Support, Amino Acid Sequence Base Pairing/drug effects/genetics Base Sequence Binding Sites/drug effects Conserved Sequence/genetics Crystallography, Bacterial/chemistry/genetics/metabolism RNA, ENNIFAR, Molecular Molecular Sequence Data *Nucleic Acid Conformation/drug effects Protein Conformation RNA, Non-U.S. Gov't Thermus thermophilus/*chemistry/genetics, Ribosomal, Unité ARN, X-Ray Magnesium/pharmacology Models},
pubstate = {published},
tppubtype = {article}
}
Romby P, Caillet J, Ebel C, Sacerdot C, Graffe M, Eyermann F, Brunel C, Moine H, Ehresmann C, Ehresmann B, Springer M
The expression of E.coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions Article de journal
Dans: EMBO J, vol. 15, no. 21, p. 5976-5987, 1996, ISBN: 8918475, (0261-4189 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon Base Sequence Binding Sites Binding, Bacterial Gene Expression Regulation, Bacterial/chemistry/genetics/metabolism RNA, Biological Molecular Sequence Data Mutagenesis, Competitive Escherichia coli/*enzymology/*genetics/metabolism Gene Expression Regulation, Enzymologic Models, Genetic, Messenger/genetics/metabolism Repressor Proteins/genetics Support, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics Translation, ROMBY, Site-Directed Nucleic Acid Conformation Operator Regions (Genetics) RNA, Unité ARN
@article{,
title = {The expression of E.coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions},
author = {P Romby and J Caillet and C Ebel and C Sacerdot and M Graffe and F Eyermann and C Brunel and H Moine and C Ehresmann and B Ehresmann and M Springer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8918475},
isbn = {8918475},
year = {1996},
date = {1996-01-01},
journal = {EMBO J},
volume = {15},
number = {21},
pages = {5976-5987},
abstract = {Threonyl-tRNA synthetase from Escherichia coli represses the translation of its own mRNA by binding to the operator region located upstream from the ribosome binding site. The operator contains two stemloop structures which interact specifically with the homodimeric enzyme. Here, we provide in vitro and in vivo evidence that these two stem-loop structures are recognized by the enzyme in an analogous way and mimic the anticodon arm of E.coli tRNA(Thr). Determination of the stoichiometry of the different RNA-threonyl-tRNA synthetase complexes reveals that two tRNA(Thr) molecules bind to the enzyme whereas only one thrS operator interacts with the homodimeric enzyme. A model is presented in which the two anticodon-like domains of the operator bind symmetrically to the two tRNA(Thr) anticodon recognition sites (one per subunit) of the dimeric threonyl-tRNA synthetase. Although symmetrical operator-repressor interactions in transcriptional control are widespread, this report stresses the importance of such interactions in translational regulation of gene expression.},
note = {0261-4189
Journal Article},
keywords = {Anticodon Base Sequence Binding Sites Binding, Bacterial Gene Expression Regulation, Bacterial/chemistry/genetics/metabolism RNA, Biological Molecular Sequence Data Mutagenesis, Competitive Escherichia coli/*enzymology/*genetics/metabolism Gene Expression Regulation, Enzymologic Models, Genetic, Messenger/genetics/metabolism Repressor Proteins/genetics Support, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics Translation, ROMBY, Site-Directed Nucleic Acid Conformation Operator Regions (Genetics) RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Romby P, Caillet J, Ebel C, Sacerdot C, Graffe M, Eyermann F, Brunel C, Moine H, Ehresmann C, Ehresmann B, Springer M
The expression of E.coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions Article de journal
Dans: EMBO J, vol. 15, no. 21, p. 5976-5987, 1996, ISBN: 8918475, (0261-4189 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon Base Sequence Binding Sites Binding, Bacterial Gene Expression Regulation, Bacterial/chemistry/genetics/metabolism RNA, Biological Molecular Sequence Data Mutagenesis, Competitive Escherichia coli/*enzymology/*genetics/metabolism Gene Expression Regulation, Enzymologic Models, Genetic, Messenger/genetics/metabolism Repressor Proteins/genetics Support, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics Translation, ROMBY, Site-Directed Nucleic Acid Conformation Operator Regions (Genetics) RNA, Unité ARN
@article{,
title = {The expression of E.coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions},
author = {P Romby and J Caillet and C Ebel and C Sacerdot and M Graffe and F Eyermann and C Brunel and H Moine and C Ehresmann and B Ehresmann and M Springer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8918475},
isbn = {8918475},
year = {1996},
date = {1996-01-01},
journal = {EMBO J},
volume = {15},
number = {21},
pages = {5976-5987},
abstract = {Threonyl-tRNA synthetase from Escherichia coli represses the translation of its own mRNA by binding to the operator region located upstream from the ribosome binding site. The operator contains two stemloop structures which interact specifically with the homodimeric enzyme. Here, we provide in vitro and in vivo evidence that these two stem-loop structures are recognized by the enzyme in an analogous way and mimic the anticodon arm of E.coli tRNA(Thr). Determination of the stoichiometry of the different RNA-threonyl-tRNA synthetase complexes reveals that two tRNA(Thr) molecules bind to the enzyme whereas only one thrS operator interacts with the homodimeric enzyme. A model is presented in which the two anticodon-like domains of the operator bind symmetrically to the two tRNA(Thr) anticodon recognition sites (one per subunit) of the dimeric threonyl-tRNA synthetase. Although symmetrical operator-repressor interactions in transcriptional control are widespread, this report stresses the importance of such interactions in translational regulation of gene expression.},
note = {0261-4189
Journal Article},
keywords = {Anticodon Base Sequence Binding Sites Binding, Bacterial Gene Expression Regulation, Bacterial/chemistry/genetics/metabolism RNA, Biological Molecular Sequence Data Mutagenesis, Competitive Escherichia coli/*enzymology/*genetics/metabolism Gene Expression Regulation, Enzymologic Models, Genetic, Messenger/genetics/metabolism Repressor Proteins/genetics Support, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics Translation, ROMBY, Site-Directed Nucleic Acid Conformation Operator Regions (Genetics) RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}