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哺乳动物铁硫蛋白在铁稳态调节和关键代谢途径中的生物合成与功能

Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.

作者信息

Rouault Tracey A, Maio Nunziata

机构信息

Molecular Medicine Branch, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.

Molecular Medicine Branch, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.

出版信息

J Biol Chem. 2017 Aug 4;292(31):12744-12753. doi: 10.1074/jbc.R117.789537. Epub 2017 Jun 14.

DOI:10.1074/jbc.R117.789537
PMID:28615439
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5546015/
Abstract

Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent binding to recipient proteins. In this minireview, we discuss how discovery of the role of the mammalian cytosolic aconitase, known as iron regulatory protein 1 (IRP1), led to the characterization of the function of its Fe-S cluster in sensing and regulating cellular iron homeostasis. Moreover, we present an overview of recent studies that have provided insights into the mechanism of Fe-S cluster transfer to recipient Fe-S proteins.

摘要

铁硫辅因子由铁和各种化学计量比的无机硫组成。一条复杂的组装途径负责它们的初始合成以及随后与受体蛋白的结合。在这篇小型综述中,我们讨论了哺乳动物胞质乌头酸酶(称为铁调节蛋白1,即IRP1)的作用的发现如何促成了对其铁硫簇在感知和调节细胞铁稳态中的功能的表征。此外,我们概述了最近的研究,这些研究为铁硫簇向受体铁硫蛋白转移的机制提供了见解。

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本文引用的文献

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Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.人 Fe-S 组装亚基的结构揭示了出乎意料的半胱氨酸脱硫酶结构和酰基-ACP-ISD11 相互作用。
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A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur Clusters to Mammalian Respiratory Chain Complexes I-III.一种单一适应性共伴侣-支架复合物将新生铁硫簇递送到哺乳动物呼吸链复合物 I-III。
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The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport.人类DNA引发酶的[4Fe4S]簇通过DNA电荷传输发挥氧化还原开关的作用。
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