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Oligomerization of the FliF domains suggests a coordinated assembly of the bacterial flagellum MS ring
bioRxiv - Biophysics Pub Date : 2021-09-23 , DOI: 10.1101/2021.09.23.461508
Giuseppina Mariano , Raquel Faba-Rodriguez , Soi Bui , Weilong Zhao , James Ross , Svetomir Tsokov , Julien Bergeron

The bacterial flagellum is a complex, self-assembling macromolecular machine that powers bacterial motility. It plays diverse roles in bacterial virulence, including aiding in colonization and dissemination during infection. The flagellum consists of a filamentous structure protruding from the cell, and the basal body, a large assembly that spans the cell envelope. The basal body is comprised of over 10 different proteins, forming several concentric ring structures, termed the M- S- L- P- and C-rings, respectively. In particular, the MS rings are formed by a single protein FliF, which consists of two trans-membrane helices anchoring it to the inner membrane and surrounding a large periplasmic domain. Assembly of the MS ring, through oligomerization of FliF, is one of the first steps of basal body assembly.

中文翻译:

FliF 结构域的寡聚化表明细菌鞭毛 MS 环的协调组装

细菌鞭毛是一种复杂的自组装大分子机器,可为细菌运动提供动力。它在细菌毒力方面发挥着不同的作用,包括在感染过程中帮助定植和传播。鞭毛由从细胞中突出的丝状结构和基体组成,基体是一个跨越细胞包膜的大组件。基体由 10 多种不同的蛋白质组成,形成几个同心环结构,分别称为 M-S-L-P-和 C-环。特别是,MS 环由单个蛋白质 FliF 形成,该蛋白质由两个跨膜螺旋组成,将其锚定在内膜并围绕一个大的周质域。通过 FliF 的寡聚化组装 MS 环是基体组装的第一步。
更新日期:2021-09-27
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