Department of Botany, The King's Buildings, University of Edinburgh, Edinburgh EH9 3JH, UK.
EMBO J. 1983;2(10):1783-9. doi: 10.1002/j.1460-2075.1983.tb01658.x.
The F(1)-ATPase complex has been purified from maize (Zea mays L.) mitochondria and shown to consist of five subunits with mol. wts. of 58 000 (alpha), 56 000 (beta), 35 000 (gamma), 22 000 (delta) and 8000 (epsilon). The alpha-subunit co-migrates on one- and two- dimensional isoelectric focussing-SDS polyacrylamide gels with the major polypeptide synthesised by isolated mitochondria. One-dimensional proteolytic peptide mapping and immunoprecipitation confirms that the alpha-subunit is a mitochondrial translation product and therefore presumably encoded in mitochondrial DNA. This contrasts with the situation in animal and fungal cells where all five subunits of the F(1)-ATPase are encoded by the nuclear genome and synthesised on cytosolic ribosomes.
F(1)-ATP 酶复合物已从玉米（Zea mays L.）线粒体中纯化，并显示由分子量为 58000（α）、56000（β）、35000（γ）、22000（δ）和 8000（ε）的五个亚基组成。α-亚基在一维和二维等电聚焦-SDS 聚丙烯酰胺凝胶中与由分离的线粒体合成的主要多肽共迁移。一维蛋白水解肽图谱和免疫沉淀证实α-亚基是线粒体翻译产物，因此推测其编码在线粒体 DNA 中。这与动物和真菌细胞中的情况形成对比，在动物和真菌细胞中，F(1)-ATP 酶的所有五个亚基都由核基因组编码，并在胞质核糖体上合成。
