Rentzsch A, Krummeck-Weiss G, Hofer A, Bartuschka A, Ostermann K, Rödel G
Institut für Genetik, Technische Universität Dresden, Mommsenstrasse 13, D-01062 Dresden, Germany.
Curr Genet. 1999 Mar;35(2):103-8. doi: 10.1007/s002940050438.
Saccharomyces cerevisiae Sco1p is believed to be involved in the transfer of copper from the carrier Cox17p to the mitochondrial cytochrome c oxidase subunits 1 and 2. We here report on the results of a mutational analysis of Sco1p. The two cysteine residues of a potential metal-binding motif (CxxxC) are essential for protein function as shown by their substitution by alanines. Chimeras consisting of Sco1p and its homolog S. cerevisiae Sco2p restrict the specificity of Sco1p function to the N-terminal half of the protein. A candidate region for conferring specificity on Sco1p is a stretch of hydrophobic amino acids, which act as a membrane anchor. In line with this suggestion is the result that alterations of individual amino acids within this region impair Sco1p function.
酿酒酵母Sco1p被认为参与了铜从载体Cox17p到线粒体细胞色素c氧化酶亚基1和2的转移过程。我们在此报告Sco1p的突变分析结果。一个潜在金属结合基序（CxxxC）的两个半胱氨酸残基对蛋白质功能至关重要，用丙氨酸取代它们就证明了这一点。由Sco1p及其同源物酿酒酵母Sco2p组成的嵌合体将Sco1p功能的特异性限制在该蛋白质的N端一半区域。赋予Sco1p特异性的一个候选区域是一段疏水氨基酸序列，它起到膜锚定的作用。与此建议相符的结果是，该区域内单个氨基酸的改变会损害Sco1p的功能。
