SecY alterations that impair membrane protein folding and generate a membrane stress.
SecY alterations that impair membrane protein folding and generate a membrane stress.
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DOI：
10.1083/jcb.200611121
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发表时间：
2007-01-29
期刊：
影响因子：
--
通讯作者：
Ito K
中科院分区：
文献类型：
--
作者：
Shimohata N;Nagamori S;Akiyama Y;Kaback HR;Ito K
我们报告了一类损害膜蛋白折叠的大肠杆菌 SecY 突变体。突变体还上调 Cpx/σE 应激反应途径。在膜蛋白生物发生中的 YidC 缺陷的响应中也观察到了类似的应激诱导，但不是对信号识别颗粒靶向缺陷的响应或对易位子丰度的简单减少的响应。与之前的观点相结合，即 Cpx 系统不仅在周质和外膜位置而且在质膜处感知蛋白质异常，推测这些 secY 突变体中会产生膜蛋白的异常状态。为了支持这一观点，LacY 的体外翻译、膜整合和折叠表明，突变的膜囊泡允许 LacY 插入，但随后不能折叠成可被构象特异性抗体识别的正常构象。结果表明，膜蛋白插入易位子后，需要正常的 SecY 功能来折叠。
We report on a class of Escherichia coli SecY mutants that impair membrane protein folding. The mutants also up-regulate the Cpx/σE stress response pathways. Similar stress induction was also observed in response to a YidC defect in membrane protein biogenesis but not in response to the signal recognition particle–targeting defect or in response to a simple reduction in the abundance of the translocon. Together with the previous contention that the Cpx system senses a protein abnormality not only at periplasmic and outer membrane locations but also at the plasma membrane, abnormal states of membrane proteins are postulated to be generated in these secY mutants. In support of this notion, in vitro translation, membrane integration, and folding of LacY reveal that mutant membrane vesicles allow the insertion of LacY but not subsequent folding into a normal conformation recognizable by conformation-specific antibodies. The results demonstrate that normal SecY function is required for the folding of membrane proteins after their insertion into the translocon.
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