期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 41, 页码 11585-11590出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1609604113
关键词
sporulation; SpoIIIAG; type III secretion system; EscJ/PrgK/FliF; SigG
资金
- NIH [GM086466]
- Agence Nationale de la Recherche (ANR) [ANR-11-BSV8-005-01 PILIPATH]
- French Infrastructure for Integrated Structural Biology Initiative (FRISBI) Grant [ANR-10-INSB-05-02]
- Grenoble Alliance for Integrated Structural Cell Biology (GRAL) Grant [ANR-10-LABX-49-01]
During spore formation in Bacillus subtilis a transenvelope complex is assembled across the double membrane that separates the mother cell and forespore. This complex (called the A-Q complex) is required to maintain forespore development and is composed of proteins with remote homology to components of type II, III, and IV secretion systems found in Gram-negative bacteria. Here, we show that one of these proteins, SpoIIIAG, which has remote homology to ring-forming proteins found in type III secretion systems, assembles into an oligomeric ring in the periplasmic-like space between the two membranes. Three-dimensional reconstruction of images generated by cryo-electron microscopy indicates that the SpoIIIAG ring has a cup-and-saucer architecture with a 6-nm central pore. Structural modeling of SpoIIIAG generated a 24-member ring with dimensions similar to those of the EM-derived saucer. Point mutations in the predicted oligomeric interface disrupted ring formation in vitro and impaired forespore gene expression and efficient spore formation in vivo. Taken together, our data provide strong support for the model in which the A-Q transenvelope complex contains a conduit that connects the mother cell and forespore. We propose that a set of stacked rings spans the intermembrane space, as has been found for type III secretion systems.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据