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Science 14 September 2001:
Vol. 293. no. 5537, pp. 2057 - 2059
DOI: 10.1126/science.1062187
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Research Articles

Inhibition of the B. subtilis Regulatory Protein TRAP by the TRAP-Inhibitory Protein, AT

Angela Valbuzzi, Charles Yanofsky*

An anti-TRAP (AT) protein, a factor of previously unknown function, conveys the metabolic signal that the cellular transfer RNA for tryptophan (tRNATrp) is predominantly uncharged. Expression of the operon encoding AT is induced by uncharged tRNATrp. 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.

Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA.
Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA.
*   To whom correspondence should be addressed. E-mail: yanofsky{at}cmgm.stanford.edu

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