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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster
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Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster

机译：人Nfu（铁硫簇支架蛋白）的亚细胞区室化及其组装[4Fe-4S]簇的能力

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iron-sulfur (Fe-S) clusters serve as cofactors in many proteins that have important redox, catalytic, and regulatory functions. In bacteria, biogenesis of Fe-S clusters is mediated by multiple gene products encoded by the isc and nif operons. In particular, genetic and biochemical studies suggest that IscU, Nfu, and IscA function as scaffold proteins for assembly and delivery of rudimentary Fe-S clusters to target proteins. Here we report the characterization of human Nfu. A combination of biochemical and spectroscopic techniques, including UV-visible absorption and Fe-57 Mossbauer spectroscopies, have been used to investigate the ability of purified human Nfu to assemble Fe-S clusters. The results suggest that Nfu can assemble approximately one labile [4Fe-4S] cluster per two Nfu monomers, and support the proposal that Nfu is an alternative scaffold protein for assembly of clusters that are subsequently used for maturation of targeted Fe-S proteins. Analyses of genomic DNA, transcripts, and translation products indicate that alternative splicing of a common pre-mRNA results in synthesis of two Nfu isoforms with distinct subcellular localizations. Isoform I is localized in the mitochondria, whereas isoform II Is present in the cytosol and the nucleus. These results, together with previous reports of subcellular distributions of isoforms of human IscS and IscU in mitochondria, cytosol, and nucleus suggest that the Fe-S cluster assembly machineries are compartmentalized in higher eukaryotes. [References: 54]
机译：铁-硫（Fe-S）簇在许多具有重要氧化还原，催化和调节功能的蛋白质中充当辅助因子。在细菌中，Fe-S簇的生物发生是由isc和nif操纵子编码的多个基因产物介导的。尤其是，遗传和生化研究表明，IscU，Nfu和IscA充当支架蛋白，用于组装和递送基本的Fe-S簇至目标蛋白。在这里，我们报告人类Nfu的表征。生化和光谱技术的结合，包括紫外线可见吸收和Fe-57 Mossbauer光谱学，已被用于研究纯化的人Nfu组装Fe-S团簇的能力。结果表明，Nfu可以每两个Nfu单体组装大约一个不稳定的[4Fe-4S]簇，并支持Nfu是组装簇的替代支架蛋白的提议，该簇随后用于目标Fe-S蛋白的成熟。基因组DNA，转录本和翻译产物的分析表明，常见的pre-mRNA的可变剪接导致合成两个具有不同亚细胞定位的Nfu同种型。异构体I位于线粒体中，而异构体II存在于细胞质和细胞核中。这些结果，加上以前的报道，关于人类IscS和IscU亚型在线粒体，细胞质和细胞核中的亚细胞分布，提示Fe-S簇组装机械在高等真核生物中是分隔的。 [参考：54]

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