Watanabe Y, Shiramizu M, Tamai Y
Department of Bioresources, Faculty of Agriculture, Ehime University.
J Biochem. 1991 Aug;110(2):237-40. doi: 10.1093/oxfordjournals.jbchem.a123563.
A plasma membrane H(+)-ATPase gene from the salt-tolerant yeast Zygosaccharomyces rouxii was isolated by probing the genomic DNA library with a labeled DNA fragment derived from the Saccharomyces cerevisiae H(+)-ATPase gene (PMA1) and the nucleotide sequence of a cloned gene was determined. The gene encoded a polypeptide of molecular weight 100,060 that consisted of 920 amino acid residues. The deduced amino acid sequence was 83% homologous to that of S. cerevisiae H(+)-ATPase and was highly similar to the conserved sequences in the plasma membrane ATPase family comprising yeast plasma membrane H(+)-ATPases. The peptide motifs involved in the ATPase functions were found in the Z. rouxii H(+)-ATPase sequence. The result of Northern analysis indicated that the size of the transcript of the Z. rouxii H(+)-ATPase gene was the same as that of S. cerevisiae PMA1.
通过用源自酿酒酵母H(+)-ATP酶基因（PMA1）的标记DNA片段探测基因组DNA文库，分离出了耐盐酵母鲁氏接合酵母的质膜H(+)-ATP酶基因，并测定了克隆基因的核苷酸序列。该基因编码一个分子量为100,060的多肽，由920个氨基酸残基组成。推导的氨基酸序列与酿酒酵母H(+)-ATP酶的氨基酸序列同源性为83%，并且与包括酵母质膜H(+)-ATP酶在内的质膜ATP酶家族中的保守序列高度相似。在鲁氏接合酵母H(+)-ATP酶序列中发现了参与ATP酶功能的肽基序。Northern分析结果表明，鲁氏接合酵母H(+)-ATP酶基因转录本的大小与酿酒酵母PMA1的相同。
