Lipids mediate supramolecular outer membrane protein assembly in bacteria.

Lipids mediate supramolecular outer membrane protein assembly in bacteria.
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DOI:
10.1126/sciadv.adc9566
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发表时间:
2022-11-04
期刊:
影响因子:
13.6
通讯作者:
--
中科院分区:
综合性期刊1区
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--
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β桶外膜蛋白(β Barrel outer membrane proteins,OMPs)是革兰氏阴性菌(Gram-negative bacteria)的一种超分子组装体,是革兰氏阴性菌(Gram-negative bacteria)的外膜蛋白(outer membrane,OM)。这种组合是如何形成的尚不清楚。在这里,通过光活化交联到大肠杆菌OM,再加上模拟,生化和生物物理分析,我们揭示了OMP在体内聚类的基础。OMPs通常被不对称脂质的环形壳包围,这些脂质介导与邻近OMPs的高级复合物。OMP组件集中在丰富的孔蛋白OmpF和OmpC上,低丰度的单体β桶,如TonB依赖性转运蛋白,被包装在其上。我们的研究揭示了OMP-脂质-OMP复合物是超分子OMP组装的基本单元,通过延伸到整个细胞表面,将OM所需的多功能性与其稳定性和不渗透性结合起来。脂质将功能多样的蛋白质拴在一起,形成维持细菌外膜稳定性的复合物。
β Barrel outer membrane proteins (OMPs) cluster into supramolecular assemblies that give function to the outer membrane (OM) of Gram-negative bacteria. How such assemblies form is unknown. Here, through photoactivatable cross-linking into the Escherichia coli OM, coupled with simulations, and biochemical and biophysical analysis, we uncover the basis for OMP clustering in vivo. OMPs are typically surrounded by an annular shell of asymmetric lipids that mediate higher-order complexes with neighboring OMPs. OMP assemblies center on the abundant porins OmpF and OmpC, against which low-abundance monomeric β barrels, such as TonB-dependent transporters, are packed. Our study reveals OMP-lipid-OMP complexes to be the basic unit of supramolecular OMP assembly that, by extending across the entire cell surface, couples the requisite multifunctionality of the OM to its stability and impermeability. Lipids tether functionally-diverse proteins together creating complexes that maintain stability of the bacterial outer membrane.
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