Hell K, Herrmann J M, Pratje E, Neupert W, Stuart R A
Institut für Physiologische Chemie der Universität München, Goethestrasse 33, 80336 Munich, Germany.
Proc Natl Acad Sci U S A. 1998 Mar 3;95(5):2250-5. doi: 10.1073/pnas.95.5.2250.
A number of nuclear encoded inner membrane proteins of mitochondria span the membrane in such a manner that their N termini are located in the intermembrane space. Many of these proteins attain this membrane orientation by undergoing an export step from the matrix across the inner membrane. This export process, which resembles bacterial N-tail export from energetic and topogenic signal requirements, is facilitated by Oxa1p, a protein that has homologues throughout prokaryotes and eukaryotes. Oxa1p, as we have previously shown, is required to export the N and C termini of the mitochondrially encoded pCoxII to the intermembrane space. We demonstrate here that imported nuclear encoded proteins physically interact with Oxa1p and depend on Oxa1p for efficient export of their N termini to the intermembrane space. Furthermore, Oxa1p interacts with nascent polypeptide chains synthesized in mitochondria, including the fully synthesized pCoxII and CoxIII species. Thus, Oxa1p represents a component of a general export machinery of the mitochondrial inner membrane.
线粒体的许多核编码内膜蛋白以其N端位于膜间隙的方式跨越内膜。这些蛋白中的许多通过从基质跨内膜的输出步骤来达到这种膜取向。这种输出过程类似于细菌从能量和拓扑信号需求进行的N端输出,由Oxa1p促进,Oxa1p是一种在原核生物和真核生物中都有同源物的蛋白质。正如我们之前所表明的,Oxa1p是将线粒体编码的pCoxII的N端和C端输出到膜间隙所必需的。我们在此证明,导入的核编码蛋白与Oxa1p发生物理相互作用,并依赖Oxa1p将其N端有效地输出到膜间隙。此外,Oxa1p与在线粒体中合成的新生多肽链相互作用,包括完全合成的pCoxII和CoxIII物种。因此,Oxa1p代表线粒体内膜一般输出机制的一个组成部分。