O'Neil Patrick K, Rollauer Sarah E, Noinaj Nicholas, Buchanan Susan K
Markey Center for Structural Biology, Department of Biological Sciences, Purdue University , West Lafayette, Indiana 47907, United States.
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health , Bethesda, Maryland 20892, United States.
Biochemistry. 2015 Oct 20;54(41):6303-11. doi: 10.1021/acs.biochem.5b00852. Epub 2015 Oct 6.
β-Barrel membrane proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria; however, exactly how they are folded and inserted remains unknown. Over the past decade, both functional and structural studies have greatly contributed to addressing this elusive mechanism. It is known that a conserved core machinery is required for each organelle, though the overall composition varies significantly. The vast majority of studies that aimed to understand the biogenesis of β-barrel membrane proteins has been conducted in Gram-negative bacteria. Here, it is the task of a multicomponent complex known as the β-barrel assembly machinery (BAM) complex to fold and insert new β-barrel membrane proteins into the outer membrane. In this review, we will discuss recent discoveries with the goal of utilizing all reported structural and functional studies to piece together a current structural model for the fully assembled BAM complex.
β-桶状膜蛋白存在于线粒体、叶绿体和革兰氏阴性菌的外膜中;然而,它们究竟是如何折叠和插入的仍不清楚。在过去十年中,功能研究和结构研究都为解决这一难以捉摸的机制做出了巨大贡献。已知每个细胞器都需要一个保守的核心机制,尽管其总体组成差异很大。绝大多数旨在了解β-桶状膜蛋白生物发生的研究都是在革兰氏阴性菌中进行的。在这里,将新的β-桶状膜蛋白折叠并插入外膜是一种称为β-桶状组装机制(BAM)复合体的多组分复合体的任务。在这篇综述中,我们将讨论最近的发现,目标是利用所有已报道的结构和功能研究来拼凑出一个完整组装的BAM复合体的当前结构模型。