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

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Date: Sept. 14, 2001
From: Science(Vol. 293, Issue 5537)
Publisher: American Association for the Advancement of Science
Document Type: Article
Length: 2,584 words

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Abstract :

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

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Gale Document Number: GALE|A78825694