%0 Journal Article
%T A Fur-like protein PerR regulates two oxidative stress response related operons dpr and metQIN in Streptococcus suis
%A Tengfei Zhang
%A Yi Ding
%A Tingting Li
%A Yun Wan
%A Wei Li
%A Huanchun Chen
%A Rui Zhou
%J BMC Microbiology
%D 2012
%I BioMed Central
%R 10.1186/1471-2180-12-85
%X In the present study, the perR gene deletion mutant ¦¤perR was constructed in Streptococcus suis serotype 2 strain SC-19, and the mutant strain ¦¤perR exhibited less sensitivity to H2O2 stress compared to the wild-type. The dpr and metQIN were found to be upregulated in the ¦¤perR strain compared with SC-19. Electrophoretic mobility shift assays showed that the promoters of dpr and metQIN could be bound by the PerR protein. These results suggest that dpr and metQIN are members of the PerR regulon of S. suis. dpr encodes a Dps-like peroxide resistance protein, and the dpr knockout strains (¦¤dpr and ¦¤dpr¦¤perR) were highly sensitive to H2O2. MetQIN is a methionine transporter, and the increased utilization of methionine in the ¦¤perR strain indirectly affected the peroxide resistance. Using a promoter¨CEGFP gene fusion reporting system, we found that the PerR regulon was induced by H2O2, and the induction was modulated by metal ions. Finally, we found that the pathogenicity of the perR mutant was attenuated and easily cleared by mice.These data strongly suggest that the Fur-like protein PerR directly regulates dpr and metQIN and plays a crucial role in oxidative stress response in S. suis.
%U http://www.biomedcentral.com/1471-2180/12/85/abstract