Cryo-EM structure of respiratory complex I reveals a link to mitochondrial sulfur metabolism
Cryo-EM structure of respiratory complex I reveals a link to mitochondrial sulfur metabolism
复制标题
DOI：
10.1016/j.bbabio.2016.09.014
复制
发表时间：
2016-12-01
影响因子：
4.3
通讯作者：
Vonck, Janet
中科院分区：
文献类型：
--
作者：
D'Imprima, Edoardo;Mills, Deryck J.;Vonck, Janet
线粒体复合物I是一种1 MDa的膜蛋白复合物，在有氧能量代谢中起核心作用。生物能量核心功能由14个中心亚基执行，这些亚基从细菌到人都是保守的。尽管最近在结构测定方面取得了进展，但我们对与线粒体复合物相关的类似于30个辅助亚基的功能的理解仍然有限。我们研究了复杂的结构，从好氧酵母解脂耶氏酵母的冷冻电子显微镜。我们在7.9埃分辨率下的密度图与解脂耶氏酵母复合体的3.6-3.9埃X射线结构非常匹配。然而，cryo-EM图表明在膜表面上方的基质臂的一侧上的另外的亚基，指向远离膜臂。密度，这是不存在于任何先前描述的复合物I结构中并且发生在约20%的颗粒中，被鉴定为辅助硫转移酶亚基ST 1。解脂耶氏酵母复合物I制剂在由ST 1催化的半胱氨酸衍生物3-巯基丙酮酸产生H2S中具有活性。因此，我们提供的证据呼吸复合物I和线粒体硫代谢之间的联系。(C)2016作者由爱思唯尔公司出版
Mitochondrial complex I is a 1 MDa membrane protein complex with a central role in aerobic energy metabolism. The bioenergetic core functions are executed by 14 central subunits that are conserved from bacteria to man. Despite recent progress in structure determination, our understanding of the function of the similar to 30 accessory subunits associated with the mitochondrial complex is still limited. We have investigated the structure of complex I from the aerobic yeast Yarrowia lipolytica by cryo-electron microscopy. Our density map at 7.9 angstrom resolution closely matches the 3.6-3.9 angstrom X-ray structure of the Yarrowia lipolytica complex. However, the cryo-EM map indicated an additional subunit on the side of the matrix arm above the membrane surface, pointing away from the membrane arm. The density, which is not present in any previously described complex I structure and occurs in about 20 % of the particles, was identified as the accessory sulfur transferase subunit ST1. The Yarrowia lipolytica complex I preparation is active in generating H2S from the cysteine derivative 3-mercaptopyruvate, catalyzed by ST1. We thus provide evidence for a link between respiratory complex I and mitochondrial sulfur metabolism. (C) 2016 The Authors. Published by Elsevier B.V.