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J Biol Chem, Vol. 274, Issue 45, 32425-32432, November 5, 1999
From the Department of Cell and Molecular Biology, Umeå
University, S-901 87 Umeå, Sweden
The Pseudomonas derived
Novel Effector Control through Modulation of a Preexisting
Binding Site of the Aromatic-responsive
54-Dependent
Regulator DmpR
54-dependent DmpR activator regulates
transcription of the (methyl)phenol catabolic dmp-operon.
DmpR is constitutively expressed, but its transcriptional promoting activity is positively controlled in direct response to the presence of
multiple aromatic effectors. Previous work has led to a model in which
effector binding by the amino-terminal region of the protein relieves
repression of an intrinsic ATPase activity essential for its
transcriptional promoting property. Here, we address whether the
observed differences in the potencies of the multiple effectors (i)
reside at the level of different aromatic binding sites, or (ii) are
mediated through differential binding affinities; furthermore, we
address whether binding of distinct aromatic effectors has different
functional consequences for DmpR activity. These questions were
addressed by comparing wild type and an effector specificity mutant of
DmpR with respect to effector binding characteristics and the ability
of aromatics to elicit ATPase activity and transcription. The results
demonstrate that six test aromatics all share a common binding site on
DmpR and that binding affinities determine the concentration at which
DmpR responds to the presence of the effector, but not the magnitude of
the responses. Interestingly, this analysis reveals that the novel
abilities of the effector specificity mutant are not primarily due to
acquisition of new binding abilities, but rather, they reside in being
able to productively couple ATPase activity to transcriptional
activation. The mechanistic implications of these findings in terms of
aromatic control of DmpR activity are discussed.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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