关键词: Arabidopsis thaliana Assembly factors Carbonic anhydrase Chlamydomonas reinhardtii Complex I Gldh Indh Mitochondria

Mesh : Binding Sites Electron Transport Complex I / chemistry ultrastructure Enzyme Activation Mitochondrial Proteins / chemistry ultrastructure Models, Chemical Molecular Dynamics Simulation Plant Proteins / chemistry ultrastructure Protein Binding Protein Conformation

来  源:   DOI:10.1016/j.bbabio.2016.01.009   PDF(Sci-hub)

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,氧化磷酸化通过几种多聚酶的操作产生ATP。质子泵复合物I(NADH:泛醌氧化还原酶)是该过程中第一个也是最复杂的酶。复合物I是由40多个亚基组成的L形酶,一个FMN分子和八个Fe-S团簇。近年来,各种模型系统中复杂I突变体的遗传和蛋白质组学分析,包括植物,对这种多聚酶的组装提供了有价值的见解。在一些关键人物的协助下,称为“装配系数”,复合体I的组装以顺序和模块化的方式进行。尽管已经确定了许多因素,它们在介导复合物I组装中的确切功能仍有待阐明。这篇综述总结了我们对植物复合物I组成和组装的最新知识,这些知识来自拟南芥和莱茵衣藻等植物模型系统的研究。植物复合物I是高度保守的,并且包含也存在于哺乳动物和真菌复合物I中的大量亚基。植物复合物I还包含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。虽然已经确定了人类复合体I的14个装配因子,只有两种蛋白质,即GLDH和INDH,已被确立为植物复合体I的真正组装因素。本文是名为“呼吸复合体I”的特刊的一部分,由VolkerZickermann和UlrichBrandt编辑。
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