Geslain R, Martin F, Delagoutte B, Cavarelli J, Gangloff J, Eriani G
In vivo selection of lethal mutations reveals two functional domains in arginyl-tRNA synthetase Article de journal
Dans: RNA, vol. 6, no. 3, p. 434-448, 2000, ISBN: 10744027, (1355-8382 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Arginine-tRNA Ligase/chemistry/*genetics Cloning, ERIANI, Fungal Genes, Fungal/genetics Kinetics Models, Lethal/*genetics Genes, Molecular Fungal Proteins/biosynthesis/genetics Gene Expression Regulation, Molecular Mutation/*genetics Peptide Fragments/chemistry/genetics Saccharomyces cerevisiae/enzymology/genetics Support, Non-U.S. Gov't, Structural, Unité ARN
@article{,
title = {In vivo selection of lethal mutations reveals two functional domains in arginyl-tRNA synthetase},
author = {R Geslain and F Martin and B Delagoutte and J Cavarelli and J Gangloff and G Eriani},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10744027},
isbn = {10744027},
year = {2000},
date = {2000-01-01},
journal = {RNA},
volume = {6},
number = {3},
pages = {434-448},
abstract = {Using random mutagenesis and a genetic screening in yeast, we isolated 26 mutations that inactivate Saccharomyces cerevisiae arginyl-tRNA synthetase (ArgRS). The mutations were identified and the kinetic parameters of the corresponding proteins were tested after purification of the expression products in Escherichia coli. The effects were interpreted in the light of the crystal structure of ArgRS. Eighteen functional residues were found around the arginine-binding pocket and eight others in the carboxy-terminal domain of the enzyme. Mutations of these residues all act by strongly impairing the rates of tRNA charging and arginine activation. Thus, ArgRS and tRNA(Arg) can be considered as a kind of ribonucleoprotein, where the tRNA, before being charged, is acting as a cofactor that activates the enzyme. Furthermore, by using different tRNA(Arg) isoacceptors and heterologous tRNA(Asp), we highlighted the crucial role of several residues of the carboxy-terminal domain in tRNA recognition and discrimination.},
note = {1355-8382
Journal Article},
keywords = {Arginine-tRNA Ligase/chemistry/*genetics Cloning, ERIANI, Fungal Genes, Fungal/genetics Kinetics Models, Lethal/*genetics Genes, Molecular Fungal Proteins/biosynthesis/genetics Gene Expression Regulation, Molecular Mutation/*genetics Peptide Fragments/chemistry/genetics Saccharomyces cerevisiae/enzymology/genetics Support, Non-U.S. Gov't, Structural, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Bergdoll M., Remy M. H., Cagnon C., Masson J. M., Dumas P.
Proline-dependent oligomerization with arm exchange Article de journal
Dans: Structure, vol. 5, no. 3, p. 391-401, 1997, (0969-2126 Journal Article).
Résumé | BibTeX | Étiquettes: *Acetyltransferases, *Dimerization, *Protein, Acid, Alignment, Amino, Aminotransferases/chemistry, Animals, Aspartate, ATPase/chemistry, Bacterial, Binding, Cattle, Chickens, Comparative, Conformation, Data, Folding, Heart/enzymology, Human, mitochondria, Models, Molecular, Mutagenesis, Na(+)-K(+)-Exchanging, Pancreatic/chemistry, Plant, Proline/*physiology, Protein, Proteins/chemistry, Pyrophosphatases/chemistry, Ribonuclease, Sequence, Site-Directed, Structural, Study, Viral, Viruses/chemistry
@article{,
title = {Proline-dependent oligomerization with arm exchange},
author = { M. Bergdoll and M. H. Remy and C. Cagnon and J. M. Masson and P. Dumas},
year = {1997},
date = {1997-01-01},
journal = {Structure},
volume = {5},
number = {3},
pages = {391-401},
abstract = {BACKGROUND: Oligomerization is often necessary for protein activity or regulation and its efficiency is fundamental for the cell. The quaternary structure of a large number of oligomers consists of protomers tightly anchored to each other by exchanged arms or swapped domains. However, nothing is known about how the arms can be kept in a favourable conformation before such an oligomerization. RESULTS: Upon examination of such quaternary structures, we observe an extremely frequent occurrence of proline residues at the point where the arm leaves the protomer. Sequence alignment and site-directed mutagenesis confirm the importance of these prolines. The conservation of these residues at the hinge regions can be explained by the constraints that they impose on polypeptide conformation and dynamics: by rigidifying the mainchain, prolines favour extended conformations of arms thus favouring oligomerization, and may prevent interaction of the arms with the core of the protomer. CONCLUSIONS: Hinge prolines can be considered as 'quaternary structure helpers'. The presence of a proline should be considered when searching for a determinant of oligomerization with arm exchange and could be used to engineer synthetic oligomers or to displace a monomers to oligomers equilibrium by mutation of this proline residue.},
note = {0969-2126
Journal Article},
keywords = {*Acetyltransferases, *Dimerization, *Protein, Acid, Alignment, Amino, Aminotransferases/chemistry, Animals, Aspartate, ATPase/chemistry, Bacterial, Binding, Cattle, Chickens, Comparative, Conformation, Data, Folding, Heart/enzymology, Human, mitochondria, Models, Molecular, Mutagenesis, Na(+)-K(+)-Exchanging, Pancreatic/chemistry, Plant, Proline/*physiology, Protein, Proteins/chemistry, Pyrophosphatases/chemistry, Ribonuclease, Sequence, Site-Directed, Structural, Study, Viral, Viruses/chemistry},
pubstate = {published},
tppubtype = {article}
}
Dumas P., Bergdoll M., Cagnon C., Masson J. M.
Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering Article de journal
Dans: EMBO J, vol. 13, no. 11, p. 2483-92, 1994, (0261-4189 Journal Article).
Résumé | BibTeX | Étiquettes: *Acetyltransferases, &, Acid, Amino, Bacterial, Bacterial/*genetics, Base, Binding, Bleomycin/*metabolism/pharmacology, Conformation, Crystallization, Crystallography, Data, Drug, Fusion, Genes, Gov't, Microbial/genetics, Models, Molecular, Mutagenesis, Non-U.S., Protein, Proteins/*chemistry/genetics/isolation, Proteins/isolation, purification, purification/metabolism, Recombinant, Relationship, Resistance, Secondary, Sequence, Site-Directed, Sites, Structural, structure, Structure-Activity, Support, X-Ray
@article{,
title = {Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering},
author = { P. Dumas and M. Bergdoll and C. Cagnon and J. M. Masson},
year = {1994},
date = {1994-01-01},
journal = {EMBO J},
volume = {13},
number = {11},
pages = {2483-92},
abstract = {The antibiotic bleomycin, a strong DNA cutting agent, is naturally produced by actinomycetes which have developed a resistance mechanism against such a lethal compound. The crystal structure, at 2.3 A resolution, of a bleomycin resistance protein of 14 kDa reveals a structure in two halves with the same alpha/beta fold despite no sequence similarity. The crystal packing shows compact dimers with a hydrophobic interface and involved in mutual chain exchange. Two independent solution studies (analytical centrifugation and light scattering) showed that this dimeric form is not a packing artefact but is indeed the functional one. Furthermore, light scattering also showed that one dimer binds two antibiotic molecules as expected. A crevice located at the dimer interface, as well as the results of a site-directed mutagenesis study, led to a model wherein two bleomycin molecules are completely sequestered by one dimer. This provides a novel insight into antibiotic resistance due to drug sequestering, and probably also into drug transport and excretion.},
note = {0261-4189
Journal Article},
keywords = {*Acetyltransferases, &, Acid, Amino, Bacterial, Bacterial/*genetics, Base, Binding, Bleomycin/*metabolism/pharmacology, Conformation, Crystallization, Crystallography, Data, Drug, Fusion, Genes, Gov't, Microbial/genetics, Models, Molecular, Mutagenesis, Non-U.S., Protein, Proteins/*chemistry/genetics/isolation, Proteins/isolation, purification, purification/metabolism, Recombinant, Relationship, Resistance, Secondary, Sequence, Site-Directed, Sites, Structural, structure, Structure-Activity, Support, X-Ray},
pubstate = {published},
tppubtype = {article}
}
Nureki O, Niimi T, Muramatsu T, Kanno H, Kohno T, Florentz C, Giege R, Yokoyama S
Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli Article de journal
Dans: J Mol Biol, vol. 236, no. 3, p. 710-724, 1994, ISBN: 8114089, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon/chemistry Base Composition Base Sequence Binding Sites Computer Graphics Escherichia coli/genetics/*metabolism Genes, Bacterial Genes, FLORENTZ, Ile/*chemistry/metabolism Support, Molecular Molecular Sequence Data *Nucleic Acid Conformation Nucleic Acid Denaturation RNA, Non-U.S. Gov't, Structural, Synthetic Isoleucine-tRNA Ligase/*metabolism Models, Transfer, Unité ARN
@article{,
title = {Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli},
author = {O Nureki and T Niimi and T Muramatsu and H Kanno and T Kohno and C Florentz and R Giege and S Yokoyama},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8114089},
isbn = {8114089},
year = {1994},
date = {1994-01-01},
journal = {J Mol Biol},
volume = {236},
number = {3},
pages = {710-724},
abstract = {Molecular recognition of Escherichia coli tRNA(Ile) by the cognate isoleucyl-tRNA synthetase (IleRS) was studied by analyses of chemical footprinting with N-nitroso-N-ethylurea and aminoacylation kinetics of variant tRNA(Ile) transcripts prepared with bacteriophage T7 RNA polymerase. IleRS binds to the acceptor, dihydrouridine (D), and anticodon stems as well as to the anticodon loop. The "complete set" of determinants for the tRNA(Ile) identity consists of most of the nucleotides in the anticodon loop (G34, A35, U36, t6A37 and A38), the discriminator nucleotide (A73), and the base-pairs in the middle of the anticodon, D and acceptor stems (C29.G41, U12.A23 and C4.G69, respectively). As for the tertiary base-pairs, two are indispensable for the isoleucylation activity, whereas the others are dispensable. Correspondingly, some of the phosphate groups of these dispensable tertiary base-pair residues were shown to be exposed to N-nitroso-N-ethylurea when tRNA(Ile) was bound with IleRS. Furthermore, deletion of the T psi C-arm only slightly impaired the tRNA(Ile) activity. Thus, it is proposed that the recognition by IleRS of all the widely distributed identity determinants is coupled with a global conformational change that involves the loosening of a particular set of tertiary base-pairs of tRNA(Ile).},
note = {0022-2836
Journal Article},
keywords = {Anticodon/chemistry Base Composition Base Sequence Binding Sites Computer Graphics Escherichia coli/genetics/*metabolism Genes, Bacterial Genes, FLORENTZ, Ile/*chemistry/metabolism Support, Molecular Molecular Sequence Data *Nucleic Acid Conformation Nucleic Acid Denaturation RNA, Non-U.S. Gov't, Structural, Synthetic Isoleucine-tRNA Ligase/*metabolism Models, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Dumas P, Bergdoll M, Cagnon C, Masson J M
Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering Article de journal
Dans: EMBO J, vol. 13, no. 11, p. 2483-2492, 1994, ISBN: 7516875, (0261-4189 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: *Acetyltransferases Amino Acid Sequence Bacterial Proteins/*chemistry/genetics/isolation & purification/metabolism Base Sequence Binding Sites Bleomycin/*metabolism/pharmacology Crystallization Crystallography, Bacterial/*genetics Models, Microbial/genetics Genes, Molecular Molecular Sequence Data Mutagenesis, Non-U.S. Gov't, Secondary Recombinant Fusion Proteins/isolation & purification Structure-Activity Relationship Support, Site-Directed Protein Conformation Protein Structure, Structural, Unité ARN, X-Ray Drug Resistance
@article{,
title = {Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering},
author = {P Dumas and M Bergdoll and C Cagnon and J M Masson},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7516875},
isbn = {7516875},
year = {1994},
date = {1994-01-01},
journal = {EMBO J},
volume = {13},
number = {11},
pages = {2483-2492},
abstract = {The antibiotic bleomycin, a strong DNA cutting agent, is naturally produced by actinomycetes which have developed a resistance mechanism against such a lethal compound. The crystal structure, at 2.3 A resolution, of a bleomycin resistance protein of 14 kDa reveals a structure in two halves with the same alpha/beta fold despite no sequence similarity. The crystal packing shows compact dimers with a hydrophobic interface and involved in mutual chain exchange. Two independent solution studies (analytical centrifugation and light scattering) showed that this dimeric form is not a packing artefact but is indeed the functional one. Furthermore, light scattering also showed that one dimer binds two antibiotic molecules as expected. A crevice located at the dimer interface, as well as the results of a site-directed mutagenesis study, led to a model wherein two bleomycin molecules are completely sequestered by one dimer. This provides a novel insight into antibiotic resistance due to drug sequestering, and probably also into drug transport and excretion.},
note = {0261-4189
Journal Article},
keywords = {*Acetyltransferases Amino Acid Sequence Bacterial Proteins/*chemistry/genetics/isolation & purification/metabolism Base Sequence Binding Sites Bleomycin/*metabolism/pharmacology Crystallization Crystallography, Bacterial/*genetics Models, Microbial/genetics Genes, Molecular Molecular Sequence Data Mutagenesis, Non-U.S. Gov't, Secondary Recombinant Fusion Proteins/isolation & purification Structure-Activity Relationship Support, Site-Directed Protein Conformation Protein Structure, Structural, Unité ARN, X-Ray Drug Resistance},
pubstate = {published},
tppubtype = {article}
}
Buttcher V, Senger B, Schumacher S, Reinbolt J, Fasiolo F
Dans: Biochem Biophys Res Commun, vol. 200, no. 1, p. 370-377, 1994, ISBN: 8166708, (0006-291x Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acyl-tRNA Ligases/metabolism Anticodon/*genetics Base Composition Base Sequence Chromosomes, Artificial, Bacterial Guanine Inversion (Genetics) Lysine-tRNA Ligase/metabolism Molecular Sequence Data Mutagenesis Nucleic Acid Conformation Plasmids RNA, Genetic Tetrahydrofolate Dehydrogenase/biosynthesis/genetics/isolation & purification Uracil, Gln/chemistry/genetics RNA, Ile/chemistry/*genetics RNA, Lys/chemistry/*genetics Saccharomyces cerevisiae/*genetics *Suppression, Structural, Transfer, Unité ARN, Yeast Escherichia coli/*genetics Genes
@article{,
title = {Modulation of the suppression efficiency and amino acid identity of an artificial yeast amber isoleucine transfer RNA in Escherichia coli by a G-U pair in the anticodon stem},
author = {V Buttcher and B Senger and S Schumacher and J Reinbolt and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8166708},
isbn = {8166708},
year = {1994},
date = {1994-01-01},
journal = {Biochem Biophys Res Commun},
volume = {200},
number = {1},
pages = {370-377},
abstract = {The artificial amber suppressor corresponding to the major isoleucine tRNA from yeast (pVBt5), when expressed in E. coli, is a poor suppressor of the amber mutation lacIam181-Z. By analysing mutant forms, we could show that this was due to the presence of a U30-G40 wobble pair in the anticodon stem of the yeast tRNA and not to the level of the heterologously expressed tRNA. Efficient suppressors were obtained by restoring a normal U30-A40 or G30-C40 Watson-Crick pair. In vivo the mutant forms are exclusively charged by the bacterial lysyl-tRNA synthetase (LysRS), whereas the original yeast amber tRNA is charged at a low level by E. coli glutaminyl-tRNA synthetase (GlnRS) and LysRS. The inversion of the U30-G40 pair also induces a loss of the Gln identity. We conclude from these experiments that the U30-G40 base pair constitutes a negative determinant for LysRS interaction which operates either at the level of complex formation or at the catalytic step. As no direct contacts are seen between GlnRS and positions 30-40 of the complexed homologous tRNA, the U30-G40 pair of pVBt5 is believed to influence aminoacylation by GlnRS indirectly, probably at the level of the anticodon loop conformation by favouring an optimal apposition of the anticodon nucleotides with the protein.},
note = {0006-291x
Journal Article},
keywords = {Amino Acyl-tRNA Ligases/metabolism Anticodon/*genetics Base Composition Base Sequence Chromosomes, Artificial, Bacterial Guanine Inversion (Genetics) Lysine-tRNA Ligase/metabolism Molecular Sequence Data Mutagenesis Nucleic Acid Conformation Plasmids RNA, Genetic Tetrahydrofolate Dehydrogenase/biosynthesis/genetics/isolation & purification Uracil, Gln/chemistry/genetics RNA, Ile/chemistry/*genetics RNA, Lys/chemistry/*genetics Saccharomyces cerevisiae/*genetics *Suppression, Structural, Transfer, Unité ARN, Yeast Escherichia coli/*genetics Genes},
pubstate = {published},
tppubtype = {article}
}
Xue H, Shen W, Giege R, Wong J T
Identity elements of tRNA(Trp). Identification and evolutionary conservation Article de journal
Dans: J Biol Chem, vol. 268, no. 13, p. 9316-9322, 1993, ISBN: 8486627, (0021-9258 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Animals Bacillus subtilis/*genetics Base Sequence Cattle Cloning, Bacterial Halobacterium/genetics Kinetics Liver/physiology Molecular Sequence Data Nucleic Acid Conformation Nucleic Acid Denaturation RNA, Molecular Comparative Study Escherichia coli/*genetics *Evolution Genes, Non-U.S. Gov't Triticum/genetics Tryptophan-tRNA Ligase/metabolism, Nucleic Acid Support, Structural, Transfer, Trp/chemistry/*genetics/metabolism Saccharomyces cerevisiae/genetics Sequence Homology, Unité ARN
@article{,
title = {Identity elements of tRNA(Trp). Identification and evolutionary conservation},
author = {H Xue and W Shen and R Giege and J T Wong},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8486627},
isbn = {8486627},
year = {1993},
date = {1993-01-01},
journal = {J Biol Chem},
volume = {268},
number = {13},
pages = {9316-9322},
abstract = {In this study, the varying reactivities of Bacillus subtilis tryptophanyl-tRNA synthetase toward prokaryotic, eukaryotic, and halophile tRNAs were employed to define the potential identity elements on tRNA(Trp). On this basis mutagenesis was performed to obtain, through in vivo heterologous expression in Escherichia coli and in vitro transcription with T7 RNA polymerase, mutant B. subtilis tRNA(Trp) for comparison with the wild-type. These comparisons served to establish G73 and the anticodon as major identity elements, and A1-U72, G5-C68, and A9 as minor identity elements. While the tryptophanyl-tRNA synthetase from B. subtilis and E. coli require G73 to function, replacement of G73 by A73 favors the enzyme from yeast. This change points to the variation of the identity elements for the same amino acid among different organisms. The similarity in these elements between B. subtilis and E. coli tryptophanyl-tRNA synthetase, however, suggests that identity elements on tRNA, like the active centers on enzymes, undergo evolutionary change at slower rates than less essential portions of the macromolecule.},
note = {0021-9258
Journal Article},
keywords = {Animals Bacillus subtilis/*genetics Base Sequence Cattle Cloning, Bacterial Halobacterium/genetics Kinetics Liver/physiology Molecular Sequence Data Nucleic Acid Conformation Nucleic Acid Denaturation RNA, Molecular Comparative Study Escherichia coli/*genetics *Evolution Genes, Non-U.S. Gov't Triticum/genetics Tryptophan-tRNA Ligase/metabolism, Nucleic Acid Support, Structural, Transfer, Trp/chemistry/*genetics/metabolism Saccharomyces cerevisiae/genetics Sequence Homology, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Oguiza J A, Malumbres M, Eriani G, Pisabarro A, Mateos L M, Martin F, Martin J F
Dans: J Bacteriol, vol. 175, no. 22, p. 7356-7362, 1993, ISBN: 8226683, (0021-9193 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Support, Amino Acid Sequence Amino Acyl-tRNA Ligases/genetics Arginine/*pharmacology Arginine-tRNA Ligase/biosynthesis/*genetics Bacteria/enzymology Brevibacterium/*enzymology/*genetics Carboxy-Lyases/*genetics Cloning, Bacterial Molecular Sequence Data Molecular Weight *Multigene Family Plasmids Restriction Mapping Sequence Homology, Bacterial/*drug effects Gene Expression Regulation, Enzymologic/drug effects *Genes, ERIANI, Molecular Comparative Study Escherichia coli/genetics/growth & development Fungi/enzymology Gene Expression Regulation, Non-U.S. Gov't, Structural, Unité ARN
@article{,
title = {A gene encoding arginyl-tRNA synthetase is located in the upstream region of the lysA gene in Brevibacterium lactofermentum: regulation of argS-lysA cluster expression by arginine},
author = {J A Oguiza and M Malumbres and G Eriani and A Pisabarro and L M Mateos and F Martin and J F Martin},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8226683},
isbn = {8226683},
year = {1993},
date = {1993-01-01},
journal = {J Bacteriol},
volume = {175},
number = {22},
pages = {7356-7362},
abstract = {The Brevibacterium lactofermentum argS gene, which encodes an arginyl-tRNA synthetase, was identified in the upstream region of the lysA gene. The cloned gene was sequenced; it encodes a 550-amino-acid protein with an M(r) of 59,797. The deduced amino acid sequence showed 28% identical and 49% similar residues when compared with the sequence of the Escherichia coli arginyl-tRNA synthetase. The B. lactofermentum enzyme showed the highly conserved motifs of class I aminoacyl-tRNA synthetases. Expression of the argS gene in B. lactofermentum and E. coli resulted in an increase in aminoacyl-tRNA synthetase activity, correlated with the presence in sodium dodecyl sulfate-polyacrylamide gels of a clear protein band that corresponds to this enzyme. One single transcript of about 3,000 nucleotides and corresponding to the B. lactofermentum argS-lysA operon was identified. The transcription of these genes is repressed by lysine and induced by arginine, showing an interesting pattern of biosynthetic interlock between the pathways of both amino acids in corynebacteria.},
note = {0021-9193
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Amino Acyl-tRNA Ligases/genetics Arginine/*pharmacology Arginine-tRNA Ligase/biosynthesis/*genetics Bacteria/enzymology Brevibacterium/*enzymology/*genetics Carboxy-Lyases/*genetics Cloning, Bacterial Molecular Sequence Data Molecular Weight *Multigene Family Plasmids Restriction Mapping Sequence Homology, Bacterial/*drug effects Gene Expression Regulation, Enzymologic/drug effects *Genes, ERIANI, Molecular Comparative Study Escherichia coli/genetics/growth & development Fungi/enzymology Gene Expression Regulation, Non-U.S. Gov't, Structural, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Graffe M, Dondon J, Caillet J, Romby P, Ehresmann C, Ehresmann B, Springer M
The specificity of translational control switched with transfer RNA identity rules Article de journal
Dans: Science, vol. 255, no. 5047, p. 994-996, 1992, ISBN: 1372129, (0036-8075 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Bacterial Genes, Bacterial Molecular Sequence Data Nucleic Acid Conformation RNA, Bacterial Proteins/metabolism Base Sequence DNA Mutational Analysis *Gene Expression Regulation, Bacterial/metabolism RNA, Genetic, Messenger/*metabolism/ultrastructure RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism *Translation, ROMBY, Structural, Thr/*metabolism Support, Transfer, Unité ARN
@article{,
title = {The specificity of translational control switched with transfer RNA identity rules},
author = {M Graffe and J Dondon and J Caillet and P Romby 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=1372129},
isbn = {1372129},
year = {1992},
date = {1992-01-01},
journal = {Science},
volume = {255},
number = {5047},
pages = {994-996},
abstract = {The interaction of Escherichia coli threonyl-transfer RNA (tRNA) synthetase with the leader sequence of its own messenger RNA inhibits ribosome binding, resulting in negative translational feedback regulation. The leader sequence resembles the substrate (tRNA(Thr)) of the enzyme, and the nucleotides that mediate the correct recognition of the leader and the tRNA may be the same. A mutation suggested by tRNA identity rules that switches the resemblance of the leader sequence from tRNA(Thr) to tRNA(Met) causes the translation of the threonyl-tRNA synthetase messenger RNA to become regulated by methionyl-tRNA synthetase. This identity swap in the leader messenger RNA indicates that tRNA identity rules may be extended to interactions of synthetases with other RNAs.},
note = {0036-8075
Journal Article},
keywords = {Bacterial Genes, Bacterial Molecular Sequence Data Nucleic Acid Conformation RNA, Bacterial Proteins/metabolism Base Sequence DNA Mutational Analysis *Gene Expression Regulation, Bacterial/metabolism RNA, Genetic, Messenger/*metabolism/ultrastructure RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism *Translation, ROMBY, Structural, Thr/*metabolism Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}