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Proteome Analysis of Bacillus subtilis When Overproducing Secretory Protein  

Jang Mi (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Department of Microbiology, Inje University)
Park Byoung-Chul (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Lee Do-Hee (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Kho Chang-Won (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Cho Sa-Yeon (College of Pharmacy, Chung-Ang University)
Lee Baek-Rak (Department of Microbiology, Inje University)
Park Sung-Goo (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Publication Information
Journal of Microbiology and Biotechnology / v.16, no.3, 2006 , pp. 368-373 More about this Journal
Abstract
Bacillus subtilis and related Bacillus species are frequently used as hosts for the mass production of recombinant proteins. Accordingly, this study examined the cellular response of B. subtilis to the overexpression of a soluble secretory protein. As such, the lichenase derived from B. cereus was overexpressed in B. subtilis, initially localized in the cytoplasm as a mature form and then secreted into the medium. Thereafter, the proteome of B. subtilis was analyzed using 2D electrophoresis and MALDI-TOF mass spectrometry. The expression of several heat-shock proteins, such as dnaK and groEL, was increased under this condition. In addition, manganese superoxide dismutase and NADH dehydrogenase were also upregulated in the lichenase-secreting B. subtilis. Therefore, it was concluded that the transient accumulation of a secreted protein in B. subtilis before secretion acted as a stress on the cell, which in turn induced the expression of various protective proteins.
Keywords
Proteome; Bacillus; lichenase; secretion;
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Times Cited By Web Of Science : 5  (Related Records In Web of Science)
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