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TAM 是一种蛋白质组装的转位和组装模块,也是潜在的磷脂转移通道。

The TAM, a Translocation and Assembly Module for protein assembly and potential conduit for phospholipid transfer.

机构信息

Centre to Impact AMR, Monash University, Melbourne, VIC, 3800, Australia.

Infection Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia.

出版信息

EMBO Rep. 2024 Apr;25(4):1711-1720. doi: 10.1038/s44319-024-00111-y. Epub 2024 Mar 11.

Abstract

The assembly of β-barrel proteins into the bacterial outer membrane is an essential process enabling the colonization of new environmental niches. The TAM was discovered as a module of the β-barrel protein assembly machinery; it is a heterodimeric complex composed of an outer membrane protein (TamA) bound to an inner membrane protein (TamB). The TAM spans the periplasm, providing a scaffold through the peptidoglycan layer and catalyzing the translocation and assembly of β-barrel proteins into the outer membrane. Recently, studies on another membrane protein (YhdP) have suggested that TamB might play a role in phospholipid transport to the outer membrane. Here we review and re-evaluate the literature covering the experimental studies on the TAM over the past decade, to reconcile what appear to be conflicting claims on the function of the TAM.

摘要

β-桶状蛋白在细菌外膜中的组装是一个重要的过程,使细菌能够在新的环境小生境中定殖。TAM 作为β-桶状蛋白组装机制的一个模块被发现,它是由一个外膜蛋白(TamA)与一个内膜蛋白(TamB)组成的异二聚体复合物。TAM 横跨周质空间,为穿过肽聚糖层提供支架,并催化β-桶状蛋白易位和组装到外膜中。最近,对另一种膜蛋白(YhdP)的研究表明,TamB 可能在外膜磷脂转运中发挥作用。在这里,我们回顾和重新评估了过去十年中关于 TAM 的实验研究文献,以调和 TAM 功能似乎相互矛盾的说法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f672/11014939/df335bc2501c/44319_2024_111_Fig1_HTML.jpg

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