Okada Y, Hashimoto T, Yoshida Y, Tagawa K
J Biochem. 1986 Jan;99(1):251-6. doi: 10.1093/oxfordjournals.jbchem.a135466.
Two proteinaceous factors, 15K and 9K proteins, which acted together to stabilize the inactivated yeast F1F0-ATPase-inhibitor complex [Hashimoto, T., et al. (1984) J. Biochem. 95, 131-136] were hardly distinguishable from the sigma and epsilon subunits, respectively, of yeast F1-ATPase by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. However, they were clearly distinguishable from these subunits by analyses of the sequences at their amino terminals and by immunoblotting combined with SDS polyacrylamide gel electrophoresis. The two stabilizing factors and an ATPase inhibitor existed in mitochondria in equimolar ratios to F1-ATPase. These three protein factors were not present in purified F1-ATPase or in F1F0-ATPase preparations, but remained in the mitochondrial membranes after extraction of F1F0-ATPase with Triton X-100. These observations strongly suggest that the two stabilizing factors and the ATPase inhibitor form a regulatory substructure of mitochondrial ATP synthase, in addition to the F1 and F0 subunits.
两种蛋白质因子，即15K和9K蛋白质，它们共同作用以稳定失活的酵母F1F0 - ATP酶 - 抑制剂复合物[桥本，T.等人（1984年）《生物化学杂志》95，131 - 136]，通过十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶电泳，它们分别与酵母F1 - ATP酶的σ和ε亚基几乎无法区分。然而，通过对它们氨基末端序列的分析以及结合SDS聚丙烯酰胺凝胶电泳的免疫印迹法，它们与这些亚基明显可区分。这两种稳定因子和一种ATP酶抑制剂在线粒体中与F1 - ATP酶以等摩尔比存在。这三种蛋白质因子不存在于纯化的F1 - ATP酶或F1F0 - ATP酶制剂中，但在用Triton X - 100提取F1F0 - ATP酶后仍保留在线粒体膜中。这些观察结果强烈表明，除了F1和F0亚基外，这两种稳定因子和ATP酶抑制剂形成了线粒体ATP合酶的一种调节亚结构。
