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线粒体 Hsp70 伴侣蛋白 Ssq1 通过形成复合物促进 Isu1 向 Grx5 转移 Fe/S 簇。

The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.

机构信息

Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35032 Marburg, Germany.

出版信息

Mol Biol Cell. 2013 Jun;24(12):1830-41. doi: 10.1091/mbc.E12-09-0644. Epub 2013 Apr 24.

DOI:10.1091/mbc.E12-09-0644
PMID:23615440
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3681689/
Abstract

The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Similar to its bacterial orthologue HscA, Ssq1 binds to the scaffold protein Isu1, thereby facilitating dissociation of the newly synthesized Fe/S cluster on Isu1 and its transfer to target apoproteins. Here we use in vivo and in vitro approaches to show that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. Grx5 binding does not stimulate the ATPase activity of Ssq1 and is most pronounced for the ADP-bound form of Ssq1, which interacts with Isu1 most tightly. The vicinity of Isu1 and Grx5 on the Hsp70 chaperone facilitates rapid Fe/S cluster transfer from Isu1 to Grx5. Grx5 and its bound Fe/S cluster are required for maturation of all cellular Fe/S proteins, regardless of the type of bound Fe/S cofactor and subcellular localization. Hence Grx5 functions as a late-acting component of the core Fe/S cluster (ISC) assembly machinery linking the Fe/S cluster synthesis reaction on Isu1 with late assembly steps involving Fe/S cluster targeting to dedicated apoproteins.

摘要

线粒体 Hsp70 伴侣蛋白 Ssq1 在铁硫（Fe/S）蛋白的成熟过程中发挥着专门的作用，这是线粒体的一个基本过程。类似于其细菌同源物 HscA，Ssq1 与支架蛋白 Isu1 结合，从而促进新合成的 Fe/S 簇在 Isu1 上的解离及其向靶蛋白的转移。在这里，我们使用体内和体外方法表明，Ssq1 还与单硫谷胱甘肽 5（Grx5）在不同于 Isu1 的结合位点相互作用。Grx5 结合不会刺激 Ssq1 的 ATP 酶活性，并且在 ADP 结合形式的 Ssq1 中最为明显，该形式与 Isu1 的结合最为紧密。Hsp70 伴侣蛋白上的 Isu1 和 Grx5 彼此靠近，有助于从 Isu1 快速将 Fe/S 簇转移到 Grx5。Grx5 及其结合的 Fe/S 簇对于所有细胞 Fe/S 蛋白的成熟都是必需的，而与结合的 Fe/S 辅因子的类型和亚细胞定位无关。因此，Grx5 作为核心 Fe/S 簇（ISC）组装机制的晚期作用成分发挥作用，将 Isu1 上的 Fe/S 簇合成反应与涉及 Fe/S 簇靶向特定无蛋白的晚期组装步骤联系起来。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/0689a42c69d6/1830fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/f0bdf90b7ae3/1830fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/1c462ee47801/1830fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/9a504f081dcc/1830fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/f9007cc49d3e/1830fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/3057950681ac/1830fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/0689a42c69d6/1830fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/f0bdf90b7ae3/1830fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/1c462ee47801/1830fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/9a504f081dcc/1830fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/f9007cc49d3e/1830fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/3057950681ac/1830fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e41/3681689/0689a42c69d6/1830fig6.jpg

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