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从嗜酸氧化亚铁硫杆菌中表达、纯化和表征铁伴侣蛋白 CyaY。

Expression, purification, and characterization of an iron chaperon protein CyaY from Acidithiobacillus ferrooxidans.

机构信息

Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, 410083, Hunan, People's Republic of China.

出版信息

Curr Microbiol. 2011 Mar;62(3):733-8. doi: 10.1007/s00284-010-9775-2.

Abstract

CyaY is the bacterial homolog of frataxin, proposed to be involved in the assembly of iron-sulfur clusters. While, the physiological iron donor for the iron-sulfur clusters assembly remains controversial. In this study, the gene of CyaY from Acidithiobacillus ferrooxidans was cloned and expressed in Escherichia coli, the protein was purified by one-step affinity chromatography to homogeneity. The CyaY protein can bind ferric iron and serve as an iron donor for the biogenesis of iron-sulfur clusters on the scaffold protein IscU in the presence of IscS and L-cysteine in vitro.

摘要

CyaY 是细菌铁氧还蛋白的同源物,据推测它参与铁硫簇的组装。然而,铁硫簇组装的生理铁供体仍存在争议。在本研究中,从嗜酸氧化亚铁硫杆菌中克隆并在大肠杆菌中表达了 CyaY 基因,该蛋白通过一步亲和层析纯化至均一性。CyaY 蛋白可以结合三价铁,并在 IscS 和 L-半胱氨酸存在的情况下,作为体外支架蛋白 IscU 上铁硫簇生物发生的铁供体。

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