Caillet J, Nogueira T, Masquida B, Winter F, Graffe M, Dock-Bregeon A C, Torres-Larios A, Sankaranarayanan R, Westhof E, Ehresmann B, Ehresmann C, Romby P, Springer M
The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression Article de journal
Dans: Mol Microbiol, vol. 47, no. 4, p. 961-974, 2003, ISBN: 12581352, (0950-382x Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acyl/chemistry/metabolism Ribosomes/metabolism Support, Bacterial Genes, Bacterial Macromolecular Systems Models, Bacterial/chemistry/metabolism RNA, Binding Sites Binding, Competitive Escherichia coli/*enzymology/*genetics Evolution, Messenger/metabolism RNA, Molecular Gene Expression Regulation, Molecular Molecular Mimicry Molecular Structure Mutation Operator Regions (Genetics) Protein Structure, Non-U.S. Gov't Threonine-tRNA Ligase/*chemistry/genetics/*metabolism, ROMBY, Tertiary Protein Subunits RNA, Transfer, Unité ARN, WESTHOF
@article{,
title = {The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression},
author = {J Caillet and T Nogueira and B Masquida and F Winter and M Graffe and A C Dock-Bregeon and A Torres-Larios and R Sankaranarayanan and E Westhof and B Ehresmann and C Ehresmann and P Romby and M Springer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12581352},
isbn = {12581352},
year = {2003},
date = {2003-01-01},
journal = {Mol Microbiol},
volume = {47},
number = {4},
pages = {961-974},
abstract = {In addition to its role in tRNA aminoacylation, Escherichia coli threonyl-tRNA synthetase is a regulatory protein which binds a site, called the operator, located in the leader of its own mRNA and inhibits translational initiation by competing with ribosome binding. This work shows that the two essential steps of regulation, operator recognition and inhibition of ribosome binding, are performed by different domains of the protein. The catalytic and the C-terminal domain of the protein are involved in binding the two anticodon arm-like structures in the operator whereas the N-terminal domain of the enzyme is responsible for the competition with the ribosome. This is the first demonstration of a modular structure for a translational repressor and is reminiscent of that of transcriptional regulators. The mimicry between the operator and tRNA, suspected on the basis of previous experiments, is further supported by the fact that identical regions of the synthetase recognize both the operator and the tRNA anticodon arm. Based on these results, and recent structural data, we have constructed a computer-derived molecular model for the operator-threonyl-tRNA synthetase complex, which sheds light on several essential aspects of the regulatory mechanism.},
note = {0950-382x
Journal Article},
keywords = {Amino Acyl/chemistry/metabolism Ribosomes/metabolism Support, Bacterial Genes, Bacterial Macromolecular Systems Models, Bacterial/chemistry/metabolism RNA, Binding Sites Binding, Competitive Escherichia coli/*enzymology/*genetics Evolution, Messenger/metabolism RNA, Molecular Gene Expression Regulation, Molecular Molecular Mimicry Molecular Structure Mutation Operator Regions (Genetics) Protein Structure, Non-U.S. Gov't Threonine-tRNA Ligase/*chemistry/genetics/*metabolism, ROMBY, Tertiary Protein Subunits RNA, Transfer, Unité ARN, WESTHOF},
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}
}
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}
}