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Volume 270, Number 21, Issue of May 26, pp. 12452-12456, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Paul Babitzke , Charles Yanofsky

A filter binding assay was used to determine the structural features of L-tryptophan required for activation of TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis. We examined the ability of L-tryptophan and 26 of its analogs to activate TRAP. Our findings show that TRAP activation by L-tryptophan is highly cooperative. We also observed that TRAP activation is stereospecific; D-tryptophan did not activate. Our results further indicate that the -amino group and the carbonyl moiety of the -carboxyl group of the ligand are required for TRAP activation and that the heterocyclic amino nitrogen of L-tryptophan greatly enhances TRAP activation. We also found that changes at several positions of the indole ring of L-tryptophan resulted in reduced TRAP activation. In addition, indole and 5-methylindole were shown to be effective competitors of L-tryptophan activation of TRAP.

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