Faculty of Life Sciences, Michael Smith Building, University of Manchester, Oxford Road, Manchester M13 9PT, United Kingdom.
J Biol Chem. 2010 Oct 15;285(42):32671-7. doi: 10.1074/jbc.M110.128256. Epub 2010 Aug 13.
Protein translocation across the endoplasmic reticulum membrane occurs at the Sec61 translocon. This has two essential subunits, the channel-forming multispanning membrane protein Sec61p/Sec61α and the tail-anchored Sss1p/Sec61γ, which has been proposed to "clamp" the channel. We have analyzed the function of Sss1p using a series of domain mutants and found that both the cytosolic and transmembrane clamp domains of Sss1p are essential for protein translocation. Our data reveal that the cytosolic domain is required for Sec61p interaction but that the transmembrane clamp domain is required to complete activation of the translocon after precursor targeting to Sec61p.
内质网膜上的蛋白易位发生在 Sec61 转运通道上。该通道由两个必需亚基组成,分别是形成通道的多跨膜蛋白 Sec61p/Sec61α和尾部锚定的 Sss1p/Sec61γ,后者被认为可以“夹住”通道。我们使用一系列结构域突变体分析了 Sss1p 的功能,发现 Sss1p 的胞质和跨膜夹区对于蛋白易位都是必需的。我们的数据表明,胞质结构域对于 Sec61p 的相互作用是必需的,但跨膜夹区对于前体靶向 Sec61p 后转运通道的完全激活是必需的。