Research Article

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

See allHide authors and affiliations

Science  14 Sep 2001:
Vol. 293, Issue 5537, pp. 2057-2059
DOI: 10.1126/science.1062187

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


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.

  • * To whom correspondence should be addressed. E-mail: yanofsky{at}

View Full Text

Stay Connected to Science