通过Sss1p与Sec61p互补片段的化学交联探究内质网转位酶的分子结构。
Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p.
作者信息
Wilkinson B M, Esnault Y, Craven R A, Skiba F, Fieschi J, K'epès F, Stirling C J
机构信息
School of Biological Sciences, University of Manchester, UK.
出版信息
EMBO J. 1997 Aug 1;16(15):4549-59. doi: 10.1093/emboj/16.15.4549.
Abstract
The heterotrimeric Sec61p complex is a key component of the protein translocation apparatus of the endoplasmic reticulum membrane. The complex characterized from yeast includes Sec61p, a 10-transmembrane-domain membrane protein which has a direct interaction with Sss1p, a small C-terminal anchor protein. In order to gain some insight into the architecture of this complex we have functionally expressed Sec61p as complementary N- and C-terminal fragments. Chemical crosslinking of Sss1p to specific Sec61p fragments in these functional combinations and suppression of sec61 mutants by over-expression of Sss1p have led to identification of the region which includes transmembrane domains TM6, TM7 and TM8 (amino acid residues L232-R406) of Sec61p as a major site of interaction with Sss1p.
摘要
异源三聚体Sec61p复合物是内质网膜蛋白转运装置的关键组成部分。从酵母中鉴定出的该复合物包含Sec61p，一种具有10个跨膜结构域的膜蛋白，它与小的C末端锚定蛋白Sss1p直接相互作用。为了深入了解该复合物的结构，我们功能性地表达了Sec61p的互补N端和C端片段。在这些功能组合中，Sss1p与特定Sec61p片段的化学交联以及通过Sss1p的过表达对sec61突变体的抑制，已导致将Sec61p的包含跨膜结构域TM6、TM7和TM8（氨基酸残基L232-R406）的区域鉴定为与Sss1p相互作用的主要位点。
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