Further characterization of functional domains of PerA, role of amino and carboxy terminal domains in DNA binding.

ABSTRACT: PerA is a key regulator of virulence genes in enteropathogenic E. coli. PerA is a member of the AraC/XylS family of transcriptional regulators that directly regulates the expression of the bfp and per operons in response to different environmental cues. Here, we characterized mutants in both the amino (NTD) and carboxy (CTD) terminal domains of PerA that affect its ability to activate the expression of the bfp and per promoters. Mutants at residues predicted to be important for DNA binding within the CTD had a significant defect in their ability to bind to the regulatory regions of the bfp and per operons and, consequently, in transcriptional activation. Notably, mutants in specific NTD residues were also impaired to bind to DNA suggesting that this domain is involved in structuring the pr

SUBMITTER: Ibarra JA 

PROVIDER: S-EPMC3581565 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature