Proteome analysis of Bacillus subtilis when overproducing secretory protein

Mi Jang, Byoung Chul Park, Do Hee Lee, Chang Won Kho, Sayeon Cho, Baek Rak Lee, Sung Goo Park

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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 protiens.

Original languageEnglish
Pages (from-to)368-373
Number of pages6
JournalJournal of Microbiology and Biotechnology
Volume16
Issue number3
StatePublished - Mar 2006
Externally publishedYes

Keywords

  • Bacillus
  • Lichenase
  • Proteome
  • Secretion

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