The Pyp regulatory proteins of Yersinia enterocolitica: functional characterization and role in signal transduction and gene expression

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During an infection of the human host, pathogenic bacteria have to sense the changing environment and react with the coordinated expression of genes that encode factors necessary for survival and virulence. We could show that the human pathogenic bacterium Yersinia enterocolitica employs the proteins PypA, PypB, and PypC to activate the transcription of the H-NS-repressed hreP gene. The HreP protease is specifically expressed during an infection and necessary for full virulence. PypB and PypC regulate additional operons coding for pili and a secretion system, respectively. While PypB and PypC are DNA binding proteins, the function of the membrane protein PypA so far remains unknown. Using molecular and genetic analyses, we will functionally characterize the Pyp proteins and study protein-DNA and protein-protein interactions. Our studies will not only result in a functional characterization of the bacterial regulators, but also shed light on signal sensing and transduction in bacterial systems related to pathogenesis.