title: Bacterial translational control at atomic resolution.
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.
authors.affiliation: UPR9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 rue Descartes, 67084 Strasbourg, France.
authors.forename: Pascale
authors.initials: P
authors.lastname: Romby
authors.forename: Mathias
authors.initials: M
authors.lastname: Springer
mesh_terms: D001483:Base Sequence; D017124:Conserved Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D008954:Models, Biological; D008958:Models, Molecular; D018716:Molecular Mimicry; D009690:Nucleic Acid Conformation; D009875:Operator Regions, Genetic; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D012363:RNA, Transfer, Thr / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism; D013914:Threonine-tRNA Ligase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
chemical_list: D012333:RNA, Messenger; D012363:RNA, Transfer, Thr; D016601:RNA-Binding Proteins; D013914:Threonine-tRNA Ligase