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A mutation mimicking post-translational acetylation of CRP at Lysine 52 creates a multitude of novel binding sites that activate transcription

ABSTRACT: As a model in the field of bacterial transcription, the structure and function of the cAMP receptor protein (CRP), a global transcription factor, has been exhaustively studied. These studies have demonstrated three contacts between CRP and RNA polymerase, of which only two were thought to activate transcription in the wild-type protein. Here we provide evidence that post-transcriptional acetylation of V. cholerae CRP engages activating region 3 leading to the hundreds of novel CRP binding sites that activate transcription of genes involved in uptake and catabolism of specific carbon sources, virulence, and biofilm formation. This establishes CRP activating region 3 as a critical mediator of association both with DNA and RNA polymerase in WT CRP.

ORGANISM(S): Vibrio cholerae

PROVIDER: GSE310654 | GEO | 2025/11/28

REPOSITORIES: GEO

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