| Literature DB >> 11976286 |
Takeshi Shimizu1, Kensuke Shima, Ken-ichi Yoshino, Kazuyoshi Yonezawa, Tohru Shimizu, Hideo Hayashi.
Abstract
The proteins under the control of the two-component system VirR/VirS in Clostridium perfringens were analyzed by using two-dimensional gel electrophoresis of the culture supernatant from the wild type and the virR mutant. Based on matrix-assisted laser desorption ionization-time of flight/mass spectrometry, seven positively regulated proteins and eight negatively regulated proteins were identified. Transcriptome analysis confirmed that 7 of the 15 proteins were regulated by the VirR/VirS system at the transcriptional level, but the remaining proteins were modified with a VirR/VirS-directed protease at the posttranslation and secretion levels. We purified and characterized the VirR/VirS-directed protease from the culture supernatant and identified it as a kind of clostripain. Because this proteolytic activity was strongly inhibited by leupeptin and antipain, it was concluded that this protease was a member of the family of cysteine proteases of C. perfringens.Entities:
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Year: 2002 PMID: 11976286 PMCID: PMC135029 DOI: 10.1128/JB.184.10.2587-2594.2002
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490