Title |
A new potential secretion pathway for recombinant proteins in Bacillus subtilis
|
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Published in |
Microbial Cell Factories, November 2015
|
DOI | 10.1186/s12934-015-0374-6 |
Pubmed ID | |
Authors |
Guangqiang Wang, Yongjun Xia, Zhennan Gu, Hao Zhang, Yong Q. Chen, Haiqin Chen, Lianzhong Ai, Wei Chen |
Abstract |
Secretion of cytoplasmic expressed proteins into growth media has significant advantages. Due to the lack of an outer membrane, Bacillus subtilis is considered as a desirable 'cell factory' for the secretion of recombinant proteins. However, bottlenecks in the classical pathway for the secretion of recombinant proteins limit its use on a wide scale. In this study, we attempted to use four typical non-classically secreted proteins as signals to export three recombinant model proteins to the culture medium. All four non-classically secreted proteins can direct the export of the intrinsically disordered nucleoskeletal-like protein (Nsp). Two of them can guide the secretion of alkaline phosphatase (PhoA). One can lead the secretion of the thermostable β-galactosidase BgaB, which cannot be secreted with the aid of typical Sec-dependent signal peptides. Our results show that the non-classically secreted proteins lead the recombinant proteins to the culture medium, and thus non-classical protein secretion pathways can be exploited as a novel secretion pathway for recombinant proteins. |
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