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J Biol Chem, Vol. 273, Issue 29, 18509-18513, July 17, 1998
From the Department of Biology, Indiana University,
Bloomington, Indiana 47405
In the purple non-sulfur bacterium
Rhodobacter capsulatus, RegA and RegB comprise a
two-component regulatory system that is required for maximal anaerobic
transcription of key photosynthesis genes. RegB is a sensor kinase that
uses ATP to phosphorylate its cognate response regulator, RegA. The
mechanism under which RegA~P influences transcription of target genes
has been unclear given that past attempts to demonstrate DNA binding
activity by isolated RegA have failed. This led to a model invoking a
role for RegA~P as an intermediate in a more complex multicomponent phosphoryl transfer cascade. In the present study, we describe the
isolation of a mutant version of RegA (RegA*) which promotes high level
expression of photosynthesis genes independent of RegB. DNase I
footprint analyses show that purified RegA* binds to the promoters of
the puf and puc operons at locations that are
consistent with RegA functioning as a transcriptional activator for
these operons. We conclude that RegA functions, like most members of the response regulator family, as a DNA-binding protein that directly affects the expression of its target genes.
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