@article{,
title = {Bacterial translational control at atomic resolution},
author = {P Romby and M Springer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12615010},
isbn = {12615010},
year = {2003},
date = {2003-01-01},
journal = {Trends Genet},
volume = {19},
number = {3},
pages = {155-161},
abstract = {Translational regulation allows rapid adaptation of protein synthesis to environmental conditions. In prokaryotes, the synthesis of many RNA-binding proteins is regulated by a translational feedback mechanism involving a competition between their natural substrate and their binding site on mRNA, which are often thought to resemble each other. This article describes the case of threonyl-tRNA synthetase, which represses the translation of its own mRNA. Recent data provide the first opportunity to describe at the atomic level both the extent and the limit of mimicry between the way this enzyme recognizes tRNA(Thr) and its regulatory site in mRNA. The data also give some clues about how the binding of the synthetase to its mRNA inhibits translation.},
note = {0168-9525
Journal Article
Review
Review, Tutorial},
keywords = {Bacterial *Gene Expression Regulation, Bacterial Models, Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics *Gene Expression Regulation, Biological Models, Enzymologic Genes, Genetic, Messenger/genetics/*metabolism RNA, Molecular Molecular Mimicry Nucleic Acid Conformation Operator Regions (Genetics) RNA, Non-U.S. Gov't Threonine-tRNA Ligase/chemistry/*genetics/metabolism *Translation, ROMBY, Thr/*metabolism RNA-Binding Proteins/metabolism Support, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Translational regulation allows rapid adaptation of protein synthesis to environmental conditions. In prokaryotes, the synthesis of many RNA-binding proteins is regulated by a translational feedback mechanism involving a competition between their natural substrate and their binding site on mRNA, which are often thought to resemble each other. This article describes the case of threonyl-tRNA synthetase, which represses the translation of its own mRNA. Recent data provide the first opportunity to describe at the atomic level both the extent and the limit of mimicry between the way this enzyme recognizes tRNA(Thr) and its regulatory site in mRNA. The data also give some clues about how the binding of the synthetase to its mRNA inhibits translation.