Navarre C, Ghislain M, Leterme S, Ferroud C, Dufour J P, Goffeau A
Unité de Biochimie Physiologique, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
J Biol Chem. 1992 Mar 25;267(9):6425-8.
The purified plasma membrane H(+)-ATPase of Schizosaccharomyces pombe and Saccharomyces cerevisiae display, in addition to the catalytic subunit of 100 kDa, a highly mobile component, soluble in chloroform/methanol. Chloroform/methanol extraction of S. cerevisiae plasma membranes led to isolation of a low molecular weight proteolipid identical to that present in purified H(+)-ATPase. NH2-terminal amino acid sequencing revealed a 38-residue polypeptide with a calculated molecular mass of 4250 Da. The polypeptide lacks the first two NH2-terminal amino acids as compared with the deduced sequence of the PMP1 gene (for plasma membrane proteolipid) isolated by hybridization with an oligonucleotide probe corresponding to an internal amino acid sequence of the proteolipid. The polypeptide is predicted to contain an NH2-terminal transmembrane segment followed by a very basic hydrophilic domain.
粟酒裂殖酵母和酿酒酵母的纯化质膜H(+)-ATP酶，除了100 kDa的催化亚基外，还显示出一种高度可移动的成分，可溶于氯仿/甲醇。用氯仿/甲醇提取酿酒酵母质膜可分离出一种低分子量的蛋白脂质，它与纯化的H(+)-ATP酶中的蛋白脂质相同。氨基末端氨基酸测序显示有一个38个残基的多肽，计算分子量为4250 Da。与通过与对应于该蛋白脂质内部氨基酸序列的寡核苷酸探针杂交分离出的PMP1基因（质膜蛋白脂质）推导序列相比，该多肽缺少前两个氨基末端氨基酸。预计该多肽含有一个氨基末端跨膜片段，其后是一个非常碱性的亲水区。
