Tzagoloff A, Akai A, Needleman R B
Proc Natl Acad Sci U S A. 1975 Jun;72(6):2054-7. doi: 10.1073/pnas.72.6.2054.
Two mutants with specific defects in cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase; EC 1.9.3.1) have been isolated from cultures of Saccharomyces cerevisiae exposed to the mutagens ethyl-methane sulfonate and Mn++. The mutations have been shown to be extranuclear by two criteria. The phenotype persists in diploids formed by a cross with a p-o strain of yeast of the opposite mating type. Tetrad analysis indicates a non-Mendelian segregation (4:0 and 0:4) of the mutations. Both mutants show a total absence of cytochrome oxidase activity and of spectral cytochromes a and as. One of the mutants has been shown to be missing a polypeptide synthesized by mitochondria. The migration of this protein on polyacrylamide gels corresponds to the highest-molecular-weight subunit of cytochrome oxidase.
从暴露于诱变剂甲磺酸乙酯和锰离子的酿酒酵母培养物中分离出了两种细胞色素c氧化酶(亚铁细胞色素c:氧氧化还原酶;EC 1.9.3.1)存在特定缺陷的突变体。通过两个标准已证明这些突变是核外的。该表型在与相反交配型的p-o酵母菌株杂交形成的二倍体中持续存在。四分体分析表明突变的分离不符合孟德尔遗传规律(4:0和0:4)。两种突变体均显示完全缺乏细胞色素氧化酶活性以及光谱细胞色素a和a3。已证明其中一个突变体缺少线粒体合成的一种多肽。该蛋白质在聚丙烯酰胺凝胶上的迁移对应于细胞色素氧化酶的最高分子量亚基。