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