Hell K, Herrmann J, Pratje E, Neupert W, Stuart R A
Institut für Physiologische Chemie der Universität München, Munich, Germany.
FEBS Lett. 1997 Dec 1;418(3):367-70. doi: 10.1016/s0014-5793(97)01412-9.
Oxa1p is a mitochondrial protein reported to be involved in the assembly of the cytochrome oxidase complex. In the absence of a functional Oxa1p, subunit II of the cytochrome oxidase accumulates as its precursor form (pCoxII). Using mitochondria isolated from a yeast strain bearing a temperature sensitive mutation in the Oxa1p, pet ts1402, we have analyzed the function of the Oxa1p protein. We demonstrate that the accumulation of pCoxII in the pet ts1402 mitochondria does not reflect a compromised Imp1p activity in this mutant. Furthermore, measurement of the membrane potential has shown it to be sufficient to support the export of CoxII from the matrix. Rather, we found that newly synthesized pCoxII accumulates in the matrix of the pet ts1402 mitochondria, because export across the inner membrane is inhibited in the pet ts1402 mitochondria. In conclusion, Oxa1p mediates the export of the N- and C-termini of the mitochondrially encoded subunit II of cytochrome oxidase from the matrix to the intermembrane space.
Oxa1p是一种线粒体蛋白,据报道它参与细胞色素氧化酶复合体的组装。在缺乏功能性Oxa1p的情况下,细胞色素氧化酶的亚基II以其前体形式(pCoxII)积累。利用从在Oxa1p中携带温度敏感突变的酵母菌株pet ts1402分离得到的线粒体,我们分析了Oxa1p蛋白的功能。我们证明,pet ts1402线粒体中pCoxII的积累并不反映该突变体中Imp1p活性受损。此外,膜电位的测量表明它足以支持CoxII从基质中输出。相反,我们发现新合成的pCoxII积累在pet ts1402线粒体的基质中,因为在pet ts1402线粒体中跨内膜的输出受到抑制。总之,Oxa1p介导细胞色素氧化酶的线粒体编码亚基II的N端和C端从基质输出到膜间隙。