Proteomic approach to characterize mitochondrial complex I from plants

Proteomic approach to characterize mitochondrial complex I from plants
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DOI:
10.1016/j.phytochem.2010.11.012
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发表时间:
2011-07-01
期刊:
影响因子:
3.8
通讯作者:
Braun, Hans-Peter
Braun, Hans-Peter
中科院分区:
生物学2区
文献类型:
--
作者:
Klodmann, Jennifer;Braun, Hans-Peter

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线粒体 NADH 脱氢酶复合物(复合物 I)是迄今为止呼吸链中最大的蛋白质复合物。牛线粒体的特征最为明显,已知该物种由 45 个不同的亚基组成。蛋白质组学分析最近首次能够系统地探索植物中的复合物 I。该酶特别大并且包含许多额外的亚基。通过各种凝胶电泳程序分离亚基并通过质谱法鉴定蛋白质,发现总共 47 种不同类型的蛋白质构成拟南芥复合体 I 的一部分。存在另一个亚基 ND4L,但由于其极端的生化特性而无法通过所采用的程序检测到。 48 个亚基中的 7 个以同工型对的形式出现,其中 6 个亚基已得到实验证明。拟南芥复合物 I 的 15 个亚基是植物特有的。其中一些类似于已知功能的酶,例如碳酸酐酶和 L-半乳糖-1,4-内酯脱氢酶 (GLDH),催化抗坏血酸生物合成的最后一步。本文旨在综述植物中复合物 I 蛋白质组成的蛋白质组学数据。此外,还对其蛋白质成分进行了蛋白质组学重新评估。 (C) 2010 Elsevier Ltd. 保留所有权利。
Mitochondrial NADH dehydrogenase complex (complex I) is by far the largest protein complex of the respiratory chain. It is best characterized for bovine mitochondria and known to consist of 45 different subunits in this species. Proteomic analyses recently allowed for the first time to systematically explore complex I from plants. The enzyme is especially large and includes numerous extra subunits. Upon subunit separation by various gel electrophoresis procedures and protein identifications by mass spectrometry, overall 47 distinct types of proteins were found to form part of Arabidopsis complex I. An additional subunit, ND4L, is present but could not be detected by the procedures employed due to its extreme biochemical properties. Seven of the 48 subunits occur in pairs of isoforms, six of which were experimentally proven. Fifteen subunits of complex I from Arabidopsis are specific for plants. Some of these resemble enzymes of known functions, e.g. carbonic anhydrases and L-galactono-1,4-lactone dehydrogenase (GLDH), which catalyzes the last step of ascorbate biosynthesis. This article aims to review proteomic data on the protein composition of complex I in plants. Furthermore, a proteomic re-evaluation on its protein constituents is presented. (C) 2010 Elsevier Ltd. All rights reserved.