Interaction proteome analysis of major intracellular serine protease 1 in Bacillus subtilis = 고초균의 단백질분해효소 상호작용단백질 분석

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Title
Interaction proteome analysis of major intracellular serine protease 1 in Bacillus subtilis = 고초균의 단백질분해효소 상호작용단백질 분석
Author(s)
Sun Young Park; Byoung Chul Park; Ah Young Lee; Chang Won Kho; S Cho; Do Hee Lee; B R Lee; P K Myung; Sung Goo Park
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 16, no. 5, pp. 804-807
Publication Year
2006
Abstract
Bacterial serine proteases, especially those from Bacillus, have been extensively studied. Intracellular serine protease 1 (Isp1) is responsible for most of the proteolytic activity in B. subtilis. To identify Isp1 substrates and study its physiological functions, a mutant of Isp1, which has lost the enzymatic activity, was, constructed. Through a GST affinity chromatographic method, several Bacillus proteins that specifically interacted with S246A mutant Isp1 protein were isolated and then identified by MALDI-TOF analysis. ClpC and elongation factor Tu (EF-Tu) were among those proteins specifically bound to mutant Isp1. In addition, several proteins involved in stationary phase adaptive response (such as RNA polymerase sigma factor, spoIIIE) were also identified. These findings led us to suggest that the major function of this serine protease, whose expression is greatly increased during the stationary phase, is to mediate transition of the cell into the stationary phase in a proper and timely manner.
Keyword
interaction proteinIsp1MALDI-TOFstationary phase
ISSN
1017-7825
Publisher
South Korea
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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