In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.
In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.
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DOI：
10.1111/j.1365-2958.2010.07487.x
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发表时间：
2011-02
影响因子：
3.6
通讯作者：
Sandkvist M
中科院分区：
文献类型：
--
作者：
Gray MD;Bagdasarian M;Hol WG;Sandkvist M
II型分泌系统是一种多蛋白复合物，跨越革兰氏阴性菌的细胞包膜，促进蛋白质的分泌，包括几种毒力因子。该系统与IV型菌毛生物发生机制同源，并含有五种蛋白质EpsG-K，称为假菌毛蛋白，它们在结构上与IV型菌毛蛋白同源。已提出主要的假阿片肽EpsG在需要ATP酶EpsE的能量依赖性过程中形成菌毛样结构。一个关键的问题是膜结合的EpsG如何与细胞质ATP酶相互作用，以及这是直接还是间接的相互作用。先前的研究已经建立了双位内膜蛋白EpsL和EpsE之间的相互作用，因此，在这项研究中，我们使用体内交联来测试EpsG与EpsL相互作用的假设。我们的研究结果表明，EpsL可能作为一个支架连接EpsG和EpsE，从而吸收ATP水解产生的能量，以支持分泌。最近发现EpsL和IV型菌毛系统中的蛋白质之间的结构同源性意味着这种相互作用可能是保守的，并且代表了II型分泌和IV型菌毛系统的重要功能相互作用。
The type II secretion system is a multi-protein complex that spans the cell envelope of gram-negative bacteria and promotes the secretion of proteins, including several virulence factors. This system is homologous to the type IV pilus biogenesis machinery and contains five proteins, EpsG-K, termed the pseudopilins that are structurally homologous to the type IV pilins. The major pseudopilin EpsG has been proposed to form a pilus-like structure in an energy-dependent process that requires the ATPase, EpsE. A key remaining question is how the membrane-bound EpsG interacts with the cytoplasmic ATPase, and if this is a direct or indirect interaction. Previous studies have established an interaction between the bitopic inner membrane protein EpsL and EpsE; therefore, in this study we used in vivo cross-linking to test the hypothesis that EpsG interacts with EpsL. Our findings suggest that EpsL may function as a scaffold to link EpsG and EpsE and thereby transduce the energy generated by ATP hydrolysis to support secretion. The recent discovery of structural homology between EpsL and a protein in the type IV pilus system implies that this interaction may be conserved and represent an important functional interaction for both the type II secretion and type IV pilus systems.
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