Mokranjac Dejana, Paschen Stefan A, Kozany Christian, Prokisch Holger, Hoppins Suzanne C, Nargang Frank E, Neupert Walter, Hell Kai
Adolf-Butenandt-Institut, Lehrstuhl für Physiologische Chemie, Ludwig-Maximilians-Universität München, Butenandtstrasse 5, D-81377 München, Germany.
EMBO J. 2003 Feb 17;22(4):816-25. doi: 10.1093/emboj/cdg090.
The preprotein translocase of the inner membrane of mitochondria (TIM23 complex) is the main entry gate for proteins of the matrix and the inner membrane. We isolated the TIM23 complex of Neurospora crassa. Besides Tim23 and Tim17, it contained a novel component, referred to as Tim50. Tim50 spans the inner membrane with a single transmembrane segment and exposes a large hydrophilic domain in the intermembrane space. Tim50 is essential for viability of yeast. Mitochondria from cells depleted of Tim50 displayed strongly reduced import kinetics of preproteins using the TIM23 complex. Tim50 could be cross-linked to preproteins that were halted at the level of the translocase of the outer membrane (TOM complex) or spanning both TOM and TIM23 complexes. We suggest that Tim50 plays a crucial role in the transfer of preproteins from the TOM complex to the TIM23 complex through the intermembrane space.
线粒体内膜前体蛋白转运酶(TIM23复合物)是基质蛋白和内膜蛋白的主要进入通道。我们分离了粗糙脉孢菌的TIM23复合物。除了Tim23和Tim17外,它还包含一个新组分,称为Tim50。Tim50通过一个单一的跨膜片段跨越内膜,并在膜间隙暴露一个大的亲水区。Tim50对酵母的生存能力至关重要。来自缺失Tim50的细胞的线粒体,使用TIM23复合物时前体蛋白的导入动力学显著降低。Tim50可以与在外膜转运酶(TOM复合物)水平停滞或跨越TOM和TIM23复合物的前体蛋白交联。我们认为Tim50在通过膜间隙将前体蛋白从TOM复合物转移到TIM23复合物的过程中起关键作用。