Cited 0 time in
- Proteome analysis of Bacillus subtilis when overproducing secretory protein = 고초균의 단백체 분석
- Mi Jang; Byoung Chul Park; Do Hee Lee; Chang Won Kho; S Cho; B R Lee; Sung Goo Park
- Bibliographic Citation
- Journal of Microbiology and Biotechnology, vol. 16, no. 3, pp. 368-373
- Publication Year
- 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 protiens.
- Korea Soc-Assoc-Inst
- Appears in Collections:
- Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
- Files in This Item:
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.