Braymer Joseph J, Lill Roland
Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg.
Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Strasse, 35043 Marburg, Germany.
J Biol Chem. 2017 Aug 4;292(31):12754-12763. doi: 10.1074/jbc.R117.787101. Epub 2017 Jun 14.
The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular functions, including genome maintenance, protein translation, energy conversion, and the antiviral response. Genetic and cell biological studies over almost 2 decades have revealed some 30 proteins involved in the synthesis of cellular [2Fe-2S] and [4Fe-4S] clusters and their incorporation into numerous apoproteins. Mechanistic aspects of Fe/S protein biogenesis continue to be elucidated by biochemical and ultrastructural investigations. Here, we review recent developments in the pursuit of constructing a comprehensive model of Fe/S protein assembly in the mitochondrion.
真核生物中铁硫(Fe/S)蛋白的生物合成是一个多阶段、多隔室的过程,对广泛的细胞功能至关重要,包括基因组维持、蛋白质翻译、能量转换和抗病毒反应。近20年来的遗传学和细胞生物学研究揭示了约30种参与细胞[2Fe-2S]和[4Fe-4S]簇合成并将其掺入众多脱辅基蛋白的蛋白质。Fe/S蛋白生物合成的机制方面仍在通过生化和超微结构研究不断阐明。在这里,我们综述了在构建线粒体中Fe/S蛋白组装综合模型方面的最新进展。