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Sequestration of a dual function DNA-binding protein by Vibrio cholerae CRP

Proc Natl Acad Sci U S A. 2022-11; 
Jacob A Gibson, Michael J Gebhardt, Renato E R S Santos, Simon L Dove, Paula I Watnick
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Monoclonal Antibody Services … coli antibody (BioLegend, 663903) at a 1:5,000 dilution, and (iv) V5-tagged proteins were detected with a monoclonal antibody (GenScript, A01724) at 1:2,000 dilution. Following … Get A Quote

摘要

Although the mechanism by which the cyclic AMP receptor protein (CRP) regulates global gene transcription has been intensively studied for decades, new discoveries remain to be made. Here, we report that, during rapid growth, CRP associates with both the well-conserved, dual-function DNA-binding protein peptidase A (PepA) and the cell membrane. These interactions are not present under nutrient-limited growth conditions, due to post-translational modification of three lysines on a single face of CRP. Although coincident DNA binding is rare, dissociation from CRP results in increased PepA occupancy at many chromosomal binding sites and differential regulation of hundreds of genes, including several encoding cycli... More

关键词

Vibrio cholerae, cAMP receptor protein, peptidase A, post-translational modification, transcription regulation