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Background  RovA is a global transcriptional regulator of gene expression in pathogenic  Yersinia . RovA levels are kept in check by a sophisticated layering of distinct transcriptional and post-transcriptional regulatory mechanisms. In the enteropathogen  Y. pseudotuberculosis , we have previously reported that the extracytoplasmic stress sensing CpxA-CpxR two-component regulatory system modulates  rovA  expression.    Methodology/Principal Findings  In this study, we characterized CpxR phosphorylation (CpxR∼P)  in vitro , and determined that phosphorylation was necessary for CpxR to efficiently bind to the PCR-amplified upstream regulatory region of  rovA . The precise CpxR∼P binding site was mapped by a nuclease protection assay and directed mutagenesis confirmed that  in vivo  binding to the  rovA  promoter inhibits transcription. Reduced RovA production was most pronounced following CpxR∼P accumulation in the  Yersinia  cytoplasm during chronic Cpx pathway activation and by the indiscriminate phosphodonor action of acetyl phosphate.    Conclusions/Significance  Cpx pathway activation restricts levels of the RovA global regulator. The regulatory influence of CpxR∼P must therefore extend well beyond periplasmic quality control in the  Yersinia  envelope, to include genes involved in environmental survival and pathogenicity.

Phosphorylated CpxR Restricts Production of the RovA Global Regulator in Yersinia pseudotuberculosis