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

Sun Young Park, Byoung Chul Park, Ah Young Lee, Chang Won Kho, Sayeon Cho, Do Hee Lee, Baek Rak Lee, Pyung Keun Myung, Sung Goo Park

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)804-807
Number of pages4
JournalJournal of Microbiology and Biotechnology
Issue number5
StatePublished - May 2006
Externally publishedYes


  • Interaction protein
  • Isp1
  • Stationary phase


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