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- Title
The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocoiitica forms a ring-shaped multimeric complex.
- Authors
Koster, Margot; Bitter, Wilbert; De Cock, Hans; Allaoui, Abdelmounaaïm; Cornelis, Guy R.; Tommassen, Jan
- Abstract
The YscC protein of <em>Yersinia enterocolitica</em> 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 <em>yscN-U</em> operon or in the <em>virG</em> gene. The VirG lipoproteln 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 ≈ 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.
- Subjects
ELECTRON microscopy; MICROSCOPY; PROTEINS; YERSINIA enterocolitica; YERSINIA; MEMBRANE proteins
- Publication
Molecular Microbiology, 1997, Vol 26, Issue 4, p789
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1046/j.1365-2958.1997.6141981.x