The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex

被引:193
作者
Koster, M
Bitter, W
deCock, H
Allaoui, A
Cornelis, GR
Tommassen, J
机构
[1] UNIV UTRECHT,INST BIOMEMEBRANES,NL-3584 CH UTRECHT,NETHERLANDS
[2] UNIV CATHOLIQUE LOUVAIN,INT INST CELLULAR & MOL PATHOL,MICROBIAL PATHOGENESIS UNIT,B-1200 BRUSSELS,BELGIUM
[3] UNIV CATHOLIQUE LOUVAIN,FAC MED,B-1200 BRUSSELS,BELGIUM
关键词
D O I
10.1046/j.1365-2958.1997.6141981.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
The YscC protein of Yersinia enterocolifica is essential for the secretion of anti-host factors, called Yops, into the extracellular environment, It belongs to a family of outer membrane proteins, collectively designated secretins, that participate in a variety of transport processes, YscC has been shown to exist as a stable oligomeric complex in the outer membrane. The production of the YscC complex is regulated by temperature and is reduced in strains carrying mutations in the yscN-U operon or in the virG gene. The VirG lipoprotein was shown to be required for efficient targeting of the complex to the outer membrane, Electron microscopy revealed that purified YscC complexes form ring-shaped structures of approximate to 20 nm with an apparent central pore. Because of the architecture of the multimer, YscC appears to represent a novel type of channel-forming proteins in the bacterial outer membrane.
引用
收藏
页码:789 / 797
页数:9
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