Mashkevich G, Repetto B, Glerum D M, Jin C, Tzagoloff A
Department of Biological Sciences, Columbia University, New York, New York 10027, USA.
J Biol Chem. 1997 May 30;272(22):14356-64. doi: 10.1074/jbc.272.22.14356.
C173 and W125 are pet mutants of Saccharomyces cerevisiae, partially deficient in cytochrome oxidase but with elevated concentrations of cytochrome c. Assays of electron transport chain enzymes indicate that the mutations exert different effects on the terminal respiratory pathway, including an inefficient transfer of electrons between the bc1 and the cytochrome oxidase complexes. A cloned gene capable of restoring respiration in C173/U1 and W125 is identical to reading frame YGR112w of yeast chromosome VII (GenBank Z72897Z72897). The encoded protein is homologous to the product of the mammalian SURF-1 gene. In view of the homology, the yeast gene has been designated SHY1 (Surf Homolog of Yeast). An antibody against the carboxyl-terminal half of Shy1p has been used to localize the protein in the inner mitochondrial membrane. Deletion of part of SHY1 produces a phenotype similar to that of G91 mutants. Disruption of SHY1 at a BamHI site, located approximately 2/3 of the way into the gene, has no obvious phenotypic consequence. This evidence, together with the ability of a carboxyl-terminal coding sequence starting from the BamHI site to complement a shy1 mutant, suggests that the Shy1p contains two domains that can be separately expressed to form a functional protein.
C173和W125是酿酒酵母的pet突变体，细胞色素氧化酶部分缺陷，但细胞色素c浓度升高。电子传递链酶的测定表明，这些突变对末端呼吸途径产生不同影响，包括bc1和细胞色素氧化酶复合物之间电子传递效率低下。一个能够恢复C173/U1和W125呼吸作用的克隆基因与酵母染色体VII的阅读框YGR112w相同（GenBank Z72897Z72897）。编码的蛋白质与哺乳动物SURF-1基因的产物同源。鉴于这种同源性，酵母基因被命名为SHY1（酵母的Surf同源物）。一种针对Shy1p羧基末端一半的抗体已被用于将该蛋白质定位在线粒体内膜中。SHY1部分缺失产生的表型与G91突变体相似。在基因大约2/3位置的BamHI位点破坏SHY1没有明显的表型后果。这一证据，连同从BamHI位点开始的羧基末端编码序列能够互补shy1突变体的能力，表明Shy1p包含两个可以分别表达以形成功能蛋白的结构域。
