F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis.
F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis.
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DOI：
10.1083/jcb.200402100
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发表时间：
2004-04-26
期刊：
影响因子：
--
通讯作者：
Driessen AJ
中科院分区：
文献类型：
--
作者：
van der Laan M;Bechtluft P;Kol S;Nouwen N;Driessen AJ
大肠杆菌YidC蛋白属于Oxa1家族的膜蛋白，其被认为促进膜蛋白的插入和组装，或者与Sec移位酶合作，或者作为单独的实体。最近，我们已经表明，YidC的耗竭导致F1F0 ATP合酶和细胞色素氧化酶的功能组装的特定缺陷。我们现在证明，在体外合成的F1F0 ATP合酶亚基C（F0C）插入到内膜囊泡需要YidC。插入不依赖于质子动力，并且仅含有YidC的蛋白脂质体催化F0c在其天然跨膜拓扑结构中的膜插入，于是其组装成大的寡聚体。共重构SecYEG对插入效率没有显著影响。值得注意的是，信号识别颗粒及其膜结合受体FtsY不是F0c膜插入所必需的。总之，在大肠杆菌中发现了一条新的膜蛋白插入途径。在大肠杆菌中YidC起着唯一的作用。
The Escherichia coli YidC protein belongs to the Oxa1 family of membrane proteins that have been suggested to facilitate the insertion and assembly of membrane proteins either in cooperation with the Sec translocase or as a separate entity. Recently, we have shown that depletion of YidC causes a specific defect in the functional assembly of F1F0 ATP synthase and cytochrome o oxidase. We now demonstrate that the insertion of in vitro–synthesized F1F0 ATP synthase subunit c (F0c) into inner membrane vesicles requires YidC. Insertion is independent of the proton motive force, and proteoliposomes containing only YidC catalyze the membrane insertion of F0c in its native transmembrane topology whereupon it assembles into large oligomers. Co-reconstituted SecYEG has no significant effect on the insertion efficiency. Remarkably, signal recognition particle and its membrane-bound receptor FtsY are not required for the membrane insertion of F0c. In conclusion, a novel membrane protein insertion pathway in E. coli is described in which YidC plays an exclusive role.
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DOI：
10.1046/j.1432-1033.2003.03531.x
发表时间：
2003-04-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Facey, SJ;Kuhn, A
通讯作者：
Kuhn, A
影响因子：
4.3
作者：
Ackerman, SH
通讯作者：
Ackerman, SH
影响因子：
3.3
作者：
He, SC;Fox, TD
通讯作者：
Fox, TD
影响因子：
3.5
作者：
Arechaga, I;Jonathan, P;Walker, JE
通讯作者：
Walker, JE
影响因子：
7.7
作者：
Beck, K;Eisner, G;Müller, M
通讯作者：
Müller, M