TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA
TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA
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DOI：
10.1046/j.1365-2958.1998.00945.x
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发表时间：
1998-07-01
影响因子：
3.6
通讯作者：
Lazzaroni, JC
中科院分区：
文献类型：
--
作者：
Clavel, T;Germon, P;Lazzaroni, JC
大肠杆菌的Tol-β蛋白参与维持外膜的完整性。TolQ、TolR和托拉的跨膜结构域在细胞质膜中相互作用，而TolB和TolA在外膜附近形成复合物。TolB和托拉的中心结构域在体外与外膜孔蛋白相互作用。在这项研究中，进行了遗传和生物化学分析，以分析TolB，Escherichia coli和细胞包膜的其他成分之间的联系。结果表明，TolB可以在体内与Lpp、OmpA和TolB交联，而Lpp与TolB和OmpA交联。分离pal和tolB突变体破坏这些蛋白质之间的一些相互作用代表了表征有助于相互作用的残基的第一种方法。我们建议，TolB和ESTA是一个多蛋白复合物的一部分，连接的肽聚糖的外膜。Tol-β蛋白可能形成跨膜复合物，使两个膜紧密靠近，并帮助一些外膜成分到达其最终目的地。
The Tol-Pal proteins of Escherichia coli are involved in maintaining outer membrane integrity. Transmembrane domains of TolQ, TolR and TolA interact in the cytoplasmic membrane, while TolB and Pal form a complex near the outer membrane. TolB and the central domain of TolA interact in vitro with the outer membrane porins. In this study, both genetic and biochemical analyses were carried out to analyse the links between TolB, Pal and other components of the cell envelope. It was shown that TolB could be cross-linked in vivo with Pal, OmpA and Lpp, while Pal was associated with TolB and OmpA. The isolation of pal and tolB mutants disrupting some interactions between these proteins represents a first approach to characterizing the residues contributing to the interactions. We propose that TolB and Pal are part of a multiprotein complex that links the peptidoglycan to the outer membrane. The Tol-Pal proteins might form trans-envelope complexes that bring the two membranes into close proximity and help some outer membrane components to reach their final destination.