Inhibition of the B. subtilis Regulatory Protein TRAP by the TRAP-Inhibitory Protein, AT
- 14 September 2001
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 293 (5537) , 2057-2059
- https://doi.org/10.1126/science.1062187
Abstract
An anti-TRAP (AT) protein, a factor of previously unknown function, conveys the metabolic signal that the cellular transfer RNA for tryptophan (tRNA Trp ) is predominantly uncharged. Expression of the operon encoding AT is induced by uncharged tRNA Trp . AT associates with TRAP, the trp operon attenuation protein, and inhibits its binding to its target RNA sequences. This relieves TRAP-mediated transcription termination and translation inhibition, increasing the rate of tryptophan biosynthesis. AT binds to TRAP primarily when it is in the tryptophan-activated state. The 53-residue AT polypeptide is homologous to the zinc-binding domain of DnaJ. The mechanisms regulating tryptophan biosynthesis in Bacillus subtilis differ from those used by Escherichia coli .Keywords
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