Publications
1992
Brunel C, Caillet J, Lesage P, Graffe M, Dondon J, Moine H, Romby P, Ehresmann C, Ehresmann B, Grunberg-Manago M, Springer M
Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors Article de journal
Dans: J Mol Biol, vol. 227, no. 3, p. 621-634, 1992, ISBN: 1383551, (0022-2836).
Résumé | Liens | BibTeX | Étiquettes: Bacterial/genetics Gene Expression Regulation, Bacterial/genetics RNA, Base Sequence Escherichia coli/genetics Gene Expression Regulation, Enzymologic/*genetics Molecular Sequence Data Mutagenesis, Genetic/*genetics, Messenger/*genetics/metabolism RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism Translation, ROMBY, Site-Directed/genetics Nucleic Acid Conformation RNA, Thr/*genetics/metabolism Recombinant Fusion Proteins/genetics Support, Transfer, Unité ARN
@article{,
title = {Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors},
author = {C Brunel and J Caillet and P Lesage and M Graffe and J Dondon and H Moine and P Romby and C Ehresmann and B Ehresmann and M Grunberg-Manago and M Springer},
url = {http://www.ncbi.nlm.nih.gov/pubmed/1383551},
doi = {10.1016/0022-2836(92)90212-3},
isbn = {1383551},
year = {1992},
date = {1992-01-01},
journal = {J Mol Biol},
volume = {227},
number = {3},
pages = {621-634},
abstract = {The expression of the gene for threonyl-tRNA synthetase (thrS) is negatively autoregulated at the translational level in Escherichia coli. The synthetase binds to a region of the thrS leader mRNA upstream from the ribosomal binding site inhibiting subsequent translation. The leader mRNA consists of four structural domains. The present work shows that mutations in these four domains affect expression and/or regulation in different ways. Domain 1, the 3' end of the leader, contains the ribosomal binding site, which appears not to be essential for synthetase binding. Mutations in this domain probably affect regulation by changing the competition between the ribosome and the synthetase for binding to the leader. Domain 2, 3' from the ribosomal binding site, is a stem and loop with structural similarities to the tRNA(Thr) anticodon arm. In tRNAs the anticodon loop is seven nucleotides long, mutations that increase or decrease the length of the anticodon-like loop of domain 2 from seven nucleotides abolish control. The nucleotides in the second and third positions of the anticodon-like sequence are essential for recognition and the nucleotide in the wobble position is not, again like tRNA(Thr). The effect of mutations in domain 3 indicate that it acts as an articulation between domains 2 and 4. Domain 4 is a stable arm that has similarities to the acceptor arm of tRNA(Thr) and is shown to be necessary for regulation. Based on this mutational analysis and previous footprinting experiments, it appears that domains 2 and 4, those analogous to tRNA(Thr), are involved in binding the synthetase which inhibits translation probably by interfering with ribosome loading at the nearby translation initiation site.},
note = {0022-2836},
keywords = {Bacterial/genetics Gene Expression Regulation, Bacterial/genetics RNA, Base Sequence Escherichia coli/genetics Gene Expression Regulation, Enzymologic/*genetics Molecular Sequence Data Mutagenesis, Genetic/*genetics, Messenger/*genetics/metabolism RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*genetics/metabolism Translation, ROMBY, Site-Directed/genetics Nucleic Acid Conformation RNA, Thr/*genetics/metabolism Recombinant Fusion Proteins/genetics Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}