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Cell-free biochemical study reveals constitutively active OmpR mutants drive transcription without EnvZ phosphorylation in Escherichia coli, highlighting an intrinsic activation mechanism.
D55Q-T83A and D55Q-G94S, two pseudorevertants of the D55Q mutant OmpR, an Escherichia coli transcriptional activator, were isolated previously by R. Brissette, K. Tsung, and M. Inouye (J. Bacteriol. 173:3749-3755, 1991). These pseudorevertant OmpR proteins were purified and examined for their function as transcriptional activators in a cell-free system with an ompF DNA fragment. These proteins were transcriptionally active, even after acid treatment, whereas the wild-type OmpR was completely inactive after the same treatment. Phosphorylation of acid-treated wild-type OmpR with an EnvZ11 membrane fraction and ATP restored transcriptional activity, whereas the activities of the mutant OmpR proteins did not change after phosphorylation.
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Bowrin et al. (1992) studied this question.
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