期刊
MOLECULAR BIOTECHNOLOGY
卷 46, 期 3, 页码 250-257出版社
HUMANA PRESS INC
DOI: 10.1007/s12033-010-9295-0
关键词
SecA; Bacillus subtilis; Protein secretion; Heterologous proteins; Alkaliphilic Bacillus sp thermostable alkaline cellulase; Human interferon alpha
In this study, we examined the effects of modifying the C-terminal region of the SecA protein on the production of heterologous proteins in Bacillus subtilis. SecA was selected as a candidate among the components of the Sec system due to its ability to interact directly with both the precursors and membrane translocases. A phylogenetic comparison demonstrated that the C-terminal region is not well conserved among eubacterial SecA proteins. The deletion of the 61 amino acids at the C-terminal region led to an 83% increase in extracellular alkaliphilic Bacillus sp. thermostable alkaline cellulase (Egl-237) activity. Moreover, the productivity of human interferon alpha (hIFN-alpha 2b) was increased by 2.2-fold compared to the wild-type SecA, by deletion of these 61 amino acids. We indicated that the deletion of the C-terminal domain (CTD) of SecA enhanced the secretion of two different heterologous protein, Egl-237 and hIFN-alpha 2b. This study provides a useful method to enhance the extracellular production of heterologous proteins in B. subtilis.
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