Kim Bae Hoon, Kim Hyeon Guk, Kim Jin Seok, Jang Jung Im, Park Yong Keun
Institute of Biotechnology, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
Laboratory of Microbial Genetics, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
Microbiology (Reading). 2007 Sep;153(Pt 9):2998-3008. doi: 10.1099/mic.0.2007/007872-0.
SipB (593 aa), one of the Salmonella invasion proteins (Sips), is secreted via the Salmonella pathogenicity island 1 (SPI-1) type III secretion system (T3SS). Here, we report the delineation of several functional regions present in the SipB protein. Our data show that residues 3-8 of the SipB protein are essential for its secretion from the bacterial cell and that the SicA chaperone, which is important to ensure stability of SipB and SipC in the bacterial cytosol, binds to SipB somewhere between amino acids 80 and100 of the SipB N-terminal region. Interestingly, the N-terminal region (residues 1-160) of SipB (SipB160) cannot be secreted via the SPI-1 T3SS, but fusion of the C-terminal amphipathic region (residues 300-593) to SipB160 can restore secretion via this system.
SipB（593个氨基酸）是沙门氏菌入侵蛋白（Sips）之一，通过沙门氏菌致病岛1（SPI-1）III型分泌系统（T3SS）分泌。在此，我们报告了SipB蛋白中几个功能区域的划分。我们的数据表明，SipB蛋白的3-8位残基对于其从细菌细胞中分泌至关重要，并且SicA伴侣蛋白（对确保SipB和SipC在细菌胞质溶胶中的稳定性很重要）在SipB N端区域的80至100个氨基酸之间的某个位置与SipB结合。有趣的是，SipB的N端区域（1-160位残基）（SipB160）不能通过SPI-1 T3SS分泌，但将C端两亲区域（300-593位残基）与SipB160融合可以恢复通过该系统的分泌。
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