Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex I from higher metazoans

被引：33

作者：

Birrell, James A. ^{[1
]}

Hirst, Judy ^{[1
]}

机构：

[1] Med Res Council Mitochondrial Biol Unit, Cambridge CB2 0XY, England

来源：

FEBS LETTERS | 2010年 / 584卷 / 19期

基金：

英国医学研究理事会;

关键词：

Complex I; Mitochondria; Mrp antiporter; NADH:ubiquinone oxidoreductase; ND2; subunit; Proton translocation; MULTIPLE SEQUENCE ALIGNMENT; NADH-UBIQUINONE REDUCTASE; MITOCHONDRIAL GENOME; OCTOCORALLIA CNIDARIA; MEMBRANE-PROTEINS; OXIDOREDUCTASE; ANTHOZOA; STOICHIOMETRY; DEHYDROGENASE; HEXACORALLIA;

D O I：

10.1016/j.febslet.2010.09.017

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Three of the conserved, membrane-bound subunits in NADH: ubiquinone oxidoreductase (complex I) are related to one another, and to Mrp sodium-proton antiporters. Recent structural analysis of two prokaryotic complexes I revealed that the three subunits each contain fourteen transmembrane helices that overlay in structural alignments: the translocation of three protons may be coordinated by a lateral helix connecting them together (Efremov, R. G., Baradaran, R. and Sazanov, L. A. (2010). The architecture of respiratory complex I. Nature 465, 441-447). Here, we show that in higher metazoans the threefold symmetry is broken by the loss of three helices from subunit ND2; possible implications for the mechanism of proton translocation are discussed. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：4247 / 4252

页数：6

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