Da. Pegues et al., PHOP PHOQ TRANSCRIPTIONAL REPRESSION OF SALMONELLA-TYPHIMURIUM INVASION GENES - EVIDENCE FOR A ROLE IN PROTEIN SECRETION/, Molecular microbiology, 17(1), 1995, pp. 169-181
Previously, the PhoP-repressed locus prgH was identified as important
for signalling epithelial cells to endocytose Salmonella typhimurium.
Characterization of prgH revealed that it is an operon of four genes e
ncoding polypeptides of 392 (prgH), 80 (prgI), 101 (prgJ) and 252 amin
o acid residues (prgK). Synthesis of the 2.6 kb prgHIJK transcript was
repressed in bacteria that activate PhoP/PhoQ, indicating that PhoP/P
hoQ regulates prgHIJK by transcriptional repression. The prgI, prgJ an
d prgK predicted gene products were similar to Shigella flexneri and Y
ersinia enterocolitica proteins required for secretion of Ipa and Yop
virulence factors. Analysis of the culture supernatants from wild-type
S. typhimurium demonstrated that at least 25 polypeptides larger than
14 kDa could be detected. In contrast, prgH1::TnphoA, phoP-constituti
ve and hil-deletion mutants had significant defects in their supernata
nt protein profiles. The invasion and supernatant protein profile defe
cts of the prgH1::TnphoA mutant were both complemented by a 5.1 kb pla
smid that included prgHIJK. These results suggest that PhoP/PhoQ regul
ates extracellular transport of proteins by transcriptional repression
of secretion determinants and that secreted proteins may be involved
in signalling epithelial cells to endocytose bacteria.