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Title 

Interaction proteome analysis of major intracellular serine protease 1 in Bacillus subtilis

 

고초균의 단백질분해효소 상호작용단백질 분석

Authors 

Sun Young ParkByoung Chul ParkAh Young LeeChang Won KhoS ChoDo Hee LeeB R LeeP K MyungSung Goo Park

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2006

Citation 

Journal of Microbiology and Biotechnology, vol. 16, no. 5, pp. 804-807

Keywords 

interaction proteinIsp1MALDI-TOFstationary phaseproteomeserine proteinaseserine proteinase 1bacillus subtilisenzyme analysisprotein protein interaction

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.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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