F(1)F(0) ATP合酶亚基c在大肠杆菌内膜中被信号识别颗粒（SRP）靶向到YidC。
F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane.
作者信息
van Bloois Edwin, Jan Haan Gert, de Gier Jan-Willem, Oudega Bauke, Luirink Joen
机构信息
Department of Molecular Microbiology, Institute of Molecular Cell Biology, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands.
出版信息
FEBS Lett. 2004 Oct 8;576(1-2):97-100. doi: 10.1016/j.febslet.2004.08.069.
Escherichia coli inner membrane proteins (IMPs) use different pathways for targeting and membrane integration. We have examined the biogenesis of the F1F0 ATP synthase subunit c, a small double spanning IMP, using complementary in vivo and in vitro approaches. The data suggest that F0c is targeted by the SRP to the membrane, where it inserts at YidC in a Sec-independent mechanism. F0c appears to be the first natural substrate of this novel pathway.
大肠杆菌内膜蛋白（IMPs）通过不同途径进行靶向定位和膜整合。我们使用体内和体外互补方法研究了F1F0 ATP合酶亚基c（一种双跨膜小IMP）的生物发生过程。数据表明，F0c通过信号识别颗粒（SRP）靶向到膜上，在那里它以一种不依赖Sec的机制插入YidC。F0c似乎是这条新途径的首个天然底物。
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