Role of SycD, the chaperone of the Yersinia yop translocators YopB and YopD

被引:117
作者
Neyt, C
Cornelis, GR
机构
[1] Catholic Univ Louvain, Christian de Duve Inst Cellular Pathol, Microbial Pathogenesis Unit, B-1200 Brussels, Belgium
[2] Catholic Univ Louvain, Fac Med, B-1200 Brussels, Belgium
关键词
D O I
10.1046/j.1365-2958.1999.01154.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Extracellular Yersinia adhering at the surface of a eukaryotic cell translocate effector Yops across the plasma membrane of the cell by a mechanism requiring YopD and YopB, the latter probably mediating pore formation. We studied the role of SycD, the intrabacterial chaperone of YopD. By producing GST-YopB hybrid proteins and SycD in Escherichia coli, we observed that SycD also binds specifically to YopB and that this binding reduces the toxicity of GST-YopB in E. coli. By analysis of a series of truncated GST-YopB proteins, we observed that SycD does not bind to a discrete segment of YopB. Using the same approach, we observed that YopD can also bind to YopB. Binding between YopB and YopD occurred even in the presence of SycD, and a complex com; posed of these three proteins could be immunoprecipitated from the cytoplasm of Yersinia. In a sycD mutant, the intracellular pool of YopB and YopD was greatly reduced unless the IcrV gene was also deleted. As LcrV is known to interact with YopB and YopD and to promote their secretion, we speculate that SycD prevents a premature association between YopB-YopD and LcrV.
引用
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页码:143 / 156
页数:14
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