The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins
The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins
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DOI：
10.1016/j.ejcb.2015.05.002
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发表时间：
2015-07-01
影响因子：
6.6
通讯作者：
Milhlenhoff, Ulrich
中科院分区：
文献类型：
--
作者：
Lill, Roland;Dutkiewicz, Rafal;Milhlenhoff, Ulrich
q1线粒体在真核生物进化过程中源自α细菌内共生体。细胞器内维持着许多细菌功能，包括脂肪酸降解、柠檬酸循环、氧化磷酸化以及血红素或硫辛酸辅助因子的合成。此外，线粒体继承了细菌的铁硫簇组装（ISC）机制。许多 ISC 成分对于细胞活力至关重要，因为它们会产生一种仍然未知的含硫化合物，用于组装细胞质和核 Fe/S 蛋白，这些蛋白在蛋白质翻译、DNA 合成和修复以及染色体分离等方面发挥重要功能。含硫化合物由线粒体 ABC 转运蛋白 Atm1（人 ABCB7）输出，并被胞质铁硫蛋白组装 (CIA) 机器的组件利用。含有线粒体而不是线粒体的生物体为真核 Fe/S 蛋白质生物合成的惊人划分提供了一个有吸引力的最小模型。线粒体通过还原进化衍生自线粒体，在此期间它们几乎失去了所有经典的线粒体任务。然而，线粒体包含所有核心 ISC 成分，这些成分可能是为了协助胞质核 Fe/S 蛋白的成熟而保留的。当前的审查主要围绕 Atml 导出流程。我们概述了输出反应的线粒体要求，总结了对 Atml 3D 结构和潜在机制的最新见解，并解释了 CIA 机器如何使用线粒体输出产物来组装胞质和核 Fe/S 蛋白。 (C) 2015 爱思唯尔有限公司。版权所有。
q1Mitochondria have been derived from alpha-bacterial endosymbionts during the evolution of eukaryotes. Numerous bacterial functions have been maintained inside the organelles including fatty acid degradation, citric acid cycle, oxidative phosphorylation, and the synthesis of heme or lipoic acid cofactors. Additionally, mitochondria have inherited the bacterial iron-sulfur cluster assembly (ISC) machinery. Many of the ISC components are essential for cell viability because they generate a still unknown, sulfur-containing compound for the assembly of cytosolic and nuclear Fe/S proteins that perform important functions in, e.g., protein translation, DNA synthesis and repair, and chromosome segregation. The sulfur-containing compound is exported by the mitochondrial ABC transporter Atm1 (human ABCB7) and utilized by components of the cytosolic iron-sulfur protein assembly (CIA) machinery. An appealing minimal model for the striking compartmentation of eukaryotic Fe/S protein biogenesis is provided by organisms that contain mitosomes instead of mitochondria. Mitosomes have been derived from mitochondria by reductive evolution, during which they have lost virtually all classical mitochondrial tasks. Nevertheless, mitosomes harbor all core ISC components which presumably have been maintained for assisting the maturation of cytosolic-nuclear Fe/S proteins. The current review is centered around the Atml export process. We present an overview on the mitochondrial requirements for the export reaction, summarize recent insights into the 3D structure and potential mechanism of Atml, and explain how the CIA machinery uses the mitochondrial export product for the assembly of cytosolic and nuclear Fe/S proteins. (C) 2015 Elsevier GmbH. All rights reserved.