Two-partner Secretion of Gram-negative Bacteria A SINGLE β-BARREL PROTEIN ENABLES TRANSPORT ACROSS THE OUTER MEMBRANE
Two-partner Secretion of Gram-negative Bacteria A SINGLE β-BARREL PROTEIN ENABLES TRANSPORT ACROSS THE OUTER MEMBRANE
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DOI：
10.1074/jbc.m111.293068
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发表时间：
2012-01-20
影响因子：
4.8
通讯作者：
Mueller, Matthias
中科院分区：
文献类型：
--
作者：
Fan, Enguo;Fiedler, Silke;Mueller, Matthias
致病细菌分泌蛋白质的机制仍然知之甚少。在革兰氏阴性菌中，双伴侣分泌途径通过其专用的“TpsB”转运体向外膜输出大量的、主要与毒力相关的“TpsA”蛋白。TpsB转运蛋白属于普遍存在的Omp85超家族，其成员参与蛋白质跨细胞膜转运或整合到细胞膜中。百日咳杆菌丝状血凝素/FhaC对是一种典型的双伴侣分泌系统。我们已经将TpsB转运蛋白FhaC重组为蛋白脂质体，并证明FhaC是其同源TpsA蛋白易位所需的唯一外膜蛋白。这是第一个用于分析革兰氏阴性菌外膜蛋白分泌的体外系统。我们的数据也为Omp85转运蛋白的蛋白质易位功能提供了明确的证据。
The mechanisms of protein secretion by pathogenic bacteria remain poorly understood. In Gram-negative bacteria, the two-partner secretion pathway exports large, mostly virulence-related "TpsA" proteins across the outer membrane via their dedicated "TpsB" transporters. TpsB transporters belong to the ubiquitous Omp85 superfamily, whose members are involved in protein translocation across, or integration into, cellular membranes. The filamentous hemagglutinin/FhaC pair of Bordetella pertussis is a model two-partner secretion system. We have reconstituted the TpsB transporter FhaC into proteoliposomes and demonstrate that FhaC is the sole outer membrane protein required for translocation of its cognate TpsA protein. This is the first in vitro system for analyzing protein secretion across the outer membrane of Gram-negative bacteria. Our data also provide clear evidence for the protein translocation function of Omp85 transporters.