Serek Justyna, Bauer-Manz Gabriele, Struhalla Gabriele, van den Berg Lambertus, Kiefer Dorothee, Dalbey Ross, Kuhn Andreas
Institute of Microbiology and Molecular Biology, University of Hohenheim, Stuttgart, Germany.
EMBO J. 2004 Jan 28;23(2):294-301. doi: 10.1038/sj.emboj.7600063. Epub 2004 Jan 22.
YidC is a recently discovered bacterial membrane protein that is related to the mitochondrial Oxa1p and the Alb3 protein of chloroplasts. These proteins are required in the membrane integration process of newly synthesized proteins that do not require the classical Sec machinery. Here we demonstrate that YidC is sufficient for the membrane integration of a Sec-independent protein. Microgram amounts of the purified single-spanning Pf3 coat protein were efficiently inserted into proteoliposomes containing the purified YidC. A mutant Pf3 coat protein with an extended hydrophobic region was inserted independently of YidC into the membrane both in vivo and in vitro, but its insertion was accelerated by YidC. These results show that YidC can function separately from the Sec translocase to integrate membrane proteins into the lipid bilayer.
YidC是一种最近发现的细菌膜蛋白,它与线粒体中的Oxa1p以及叶绿体中的Alb3蛋白相关。这些蛋白在新合成的、不需要经典Sec机制的蛋白质的膜整合过程中是必需的。在此我们证明,YidC足以实现一种不依赖Sec的蛋白质的膜整合。微克量的纯化单跨膜Pf3外壳蛋白能高效插入含有纯化YidC的蛋白脂质体中。一种具有延长疏水区域的突变型Pf3外壳蛋白,在体内和体外均可独立于YidC插入膜中,但其插入过程会被YidC加速。这些结果表明,YidC可以独立于Sec转位酶发挥作用,将膜蛋白整合到脂质双层中。