期刊
EMBO JOURNAL
卷 38, 期 18, 页码 -出版社
WILEY
DOI: 10.15252/embj.2018100825
关键词
ImpA_N domain proteins; protein localization; protein-protein interactions; sheath assembly; type VI secretion system
资金
- Swiss National Science Foundation [BSSGI0_155778, 31003A_159525]
- University of Basel
- Swiss National Science Foundation (SNF) [BSSGI0_155778, 31003A_159525] Funding Source: Swiss National Science Foundation (SNF)
Protein translocation by the bacterial type VI secretion system (T6SS) is driven by a rapid contraction of a sheath assembled around a tube with associated effectors. Here, we show that TssA-like or TagA-like proteins with a conserved N-terminal domain and varying C-terminal domains can be grouped into at least three distinct classes based on their role in sheath assembly. The proteins of the first class increase speed and frequency of sheath assembly and form a stable dodecamer at the distal end of a polymerizing sheath. The proteins of the second class localize to the cell membrane and block sheath polymerization upon extension across the cell. This prevents excessive sheath polymerization and bending, which may result in sheath destabilization and detachment from its membrane anchor and thus result in failed secretion. The third class of these proteins localizes to the baseplate and is required for initiation of sheath assembly. Our work shows that while various proteins share a conserved N-terminal domain, their roles in T6SS biogenesis are fundamentally different.
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