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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.
Structural
Features of L-Tryptophan Required for Activation of TRAP, the
trp RNA-binding Attenuation Protein of Bacillus
subtilis
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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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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