Brambl R, Plesofsky-Vig N
Proc Natl Acad Sci U S A. 1986 Jun;83(11):3644-8. doi: 10.1073/pnas.83.11.3644.
One polypeptide subunit of cytochrome c oxidase (EC 1.9.3.1) and two subunits of the ATPase/ATP synthase (EC 3.6.1.34) in mitochondria of Neurospora crassa are covalently modified with a derivative of pantothenic acid. In asexual spores of a pantothenate auxotroph of Neurospora, deprivation of pantothenic acid blocked the increase of the specific activities of cytochrome c oxidase and the ATPase above the basal activities in the dormant spores. Under cellular panthothenate deprivation, all the subunit peptides of these two enzymes apparently were synthesized and accumulated in the mitochondria, but these subunits were not assembled into normal complexes, and 55Fe-labeled heme a was incorporated into immunoprecipitable cytochrome c oxidase to a very low extent. In pantothenate-supplemented cells, the pantothenate derivative apparently is attached to the free unassembled subunits and appears not to be present in the assembled enzymes. It is likely that cellular deprivation of pantothenate, resulting in failure to modify the three subunit peptides, causes an interruption of the assembly pathway of cytochrome c oxidase and the ATPase/ATP synthase.
粗糙脉孢菌线粒体中的细胞色素c氧化酶(EC 1.9.3.1)的一个多肽亚基和ATP酶/ATP合酶(EC 3.6.1.34)的两个亚基被泛酸衍生物共价修饰。在粗糙脉孢菌泛酸盐营养缺陷型的无性孢子中,泛酸缺乏会阻止细胞色素c氧化酶和ATP酶的比活性在休眠孢子的基础活性之上增加。在细胞泛酸盐缺乏的情况下,这两种酶的所有亚基肽显然都在线粒体中合成并积累,但这些亚基没有组装成正常的复合物,并且55Fe标记的血红素a仅以非常低的程度掺入可免疫沉淀的细胞色素c氧化酶中。在补充泛酸盐的细胞中,泛酸衍生物显然附着在游离的未组装亚基上,并且似乎不存在于组装好的酶中。很可能细胞泛酸盐缺乏导致无法修饰这三个亚基肽,从而导致细胞色素c氧化酶和ATP酶/ATP合酶的组装途径中断。