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植物线粒体复合体I的组成与组装:综述

Plant mitochondrial Complex I composition and assembly: A review.

作者信息

Subrahmanian Nitya, Remacle Claire, Hamel Patrice Paul

机构信息

The Ohio State University, Department of Molecular Genetics, 500 Aronoff Laboratory, 318 W. 12th Avenue, Columbus, OH 43210, USA.

Institute of Botany, Department of Life Sciences, University of Liège, 4000 Liège, Belgium.

出版信息

Biochim Biophys Acta. 2016 Jul;1857(7):1001-14. doi: 10.1016/j.bbabio.2016.01.009. Epub 2016 Jan 19.

Abstract

In the mitochondrial inner membrane, oxidative phosphorylation generates ATP via the operation of several multimeric enzymes. The proton-pumping Complex I (NADH:ubiquinone oxidoreductase) is the first and most complicated enzyme required in this process. Complex I is an L-shaped enzyme consisting of more than 40 subunits, one FMN molecule and eight Fe-S clusters. In recent years, genetic and proteomic analyses of Complex I mutants in various model systems, including plants, have provided valuable insights into the assembly of this multimeric enzyme. Assisted by a number of key players, referred to as "assembly factors", the assembly of Complex I takes place in a sequential and modular manner. Although a number of factors have been identified, their precise function in mediating Complex I assembly still remains to be elucidated. This review summarizes our current knowledge of plant Complex I composition and assembly derived from studies in plant model systems such as Arabidopsis thaliana and Chlamydomonas reinhardtii. Plant Complex I is highly conserved and comprises a significant number of subunits also present in mammalian and fungal Complexes I. Plant Complex I also contains additional subunits absent from the mammalian and fungal counterpart, whose function in enzyme activity and assembly is not clearly understood. While 14 assembly factors have been identified for human Complex I, only two proteins, namely GLDH and INDH, have been established as bona fide assembly factors for plant Complex I. This article is part of a Special Issue entitled Respiratory complex I, edited by Volker Zickermann and Ulrich Brandt.

摘要

在线粒体内膜中,氧化磷酸化通过几种多聚体酶的作用产生ATP。质子泵复合物I(NADH:泛醌氧化还原酶)是此过程中所需的首个也是最复杂的酶。复合物I是一种L形酶,由40多个亚基、一个FMN分子和八个铁硫簇组成。近年来,对包括植物在内的各种模型系统中复合物I突变体的遗传和蛋白质组学分析,为这种多聚体酶的组装提供了有价值的见解。在一些被称为“组装因子”的关键参与者的协助下,复合物I的组装以有序和模块化的方式进行。尽管已经鉴定出许多因子,但其在介导复合物I组装中的精确功能仍有待阐明。本综述总结了我们目前从拟南芥和莱茵衣藻等植物模型系统的研究中获得的关于植物复合物I组成和组装的知识。植物复合物I高度保守,包含大量也存在于哺乳动物和真菌复合物I中的亚基。植物复合物I还含有哺乳动物和真菌对应物中不存在的其他亚基,其在酶活性和组装中的功能尚不清楚。虽然已为人复合物I鉴定出14种组装因子,但仅两种蛋白质,即谷氨酸脱氢酶(GLDH)和异柠檬酸脱氢酶(INDH),已被确定为植物复合物I真正的组装因子。本文是由Volker Zickermann和Ulrich Brandt编辑的名为《呼吸复合物I》的特刊的一部分。

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