Symmetrical interactions between the translational operator of the thrS gene and dimeric threonyl transfer RNA synthetase.
Threonyl-tRNA synthetase from Escherichia coli represses the translation of its coding gene, thrS, by binding an operator located in the leader region of its messenger RNA. Published data on the structure of this leader region and on its interaction with threonyl-tRNA synthetase support a model in which each of two stem-and-loop structures mimics the anticodon arm of tRNA(Thr) and binds a different subunit of one synthetase dimer.
Bedouelle
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Groupe d'Ingénierie des Protéines (CNRS URA 1129), Unité de Biochimie Cellulaire, Institut Pasteur, Paris, France.
D000926:Anticodon; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D008969:Molecular Sequence Data; D009875:Operator Regions, Genetic; D011485:Protein Binding; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012329:RNA, Bacterial / Q000378:metabolism; D013914:Threonine-tRNA Ligase / Q000235:genetics* / Q000378:metabolism
D000926:Anticodon; D012329:RNA, Bacterial; D013914:Threonine-tRNA Ligase