Lode A, Kuschel M, Paret C, Rödel G
Institute of Genetics, University of Technology Dresden, Mommsenstrasse 13, D-01062 Dresden, Germany.
FEBS Lett. 2000 Nov 17;485(1):19-24. doi: 10.1016/s0014-5793(00)02176-1.
Yeast mitochondrial Sco1p is required for the formation of a functional cytochrome c oxidase (COX). It was suggested that Sco1p aids copper delivery to the catalytic center of COX. Here we show by affinity chromatography and coimmunoprecipitation that Sco1p interacts with subunit Cox2p. In addition we provide evidence that Sco1p can form homomeric complexes. Both homomer formation and binding of Cox2p are neither dependent on the presence of copper nor affected by mutations of His-239, Cys-148 or Cys-152. These amino acids, which are conserved among the members of the Sco1p family, have been suggested to act in the reduction of the cysteines in the copper binding center of Cox2p and are discussed as ligands for copper.
酵母线粒体Sco1p是功能性细胞色素c氧化酶（COX）形成所必需的。有人提出Sco1p有助于将铜传递到COX的催化中心。在这里，我们通过亲和层析和免疫共沉淀表明Sco1p与亚基Cox2p相互作用。此外，我们提供证据表明Sco1p可以形成同聚复合物。同聚体形成和Cox2p的结合既不依赖于铜的存在，也不受His-239、Cys-148或Cys-152突变的影响。这些在Sco1p家族成员中保守的氨基酸，被认为在Cox2p铜结合中心的半胱氨酸还原中起作用，并被讨论为铜的配体。
