Cytosolic iron-sulfur cluster transfer-a proposed kinetic pathway for reconstitution of glutaredoxin 3

被引：22
|
作者：
Wachnowsky, Christine [1 ,2 ]
Fidai, Insiya [1 ,3 ]
Cowan, James A. [1 ,2 ,3 ]
机构：
[1] Ohio State Univ, Dept Chem & Biochem, 100 West 18th Ave, Columbus, OH 43210 USA
[2] Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA
[3] Ohio State Univ, Biophys Grad Program, Columbus, OH 43210 USA
来源：
FEBS LETTERS | 2016年 / 590卷 / 24期
基金：
美国国家卫生研究院;
关键词：
2Fe-2S] cluster transfer; glutaredoxin; iron-sulfur cluster; IscU; Nfu; MONOTHIOL GLUTAREDOXINS; SACCHAROMYCES-CEREVISIAE; 4FE-4S CLUSTER; 2FE-2S CLUSTER; HUMAN NFU; PROTEIN BIOGENESIS; SCAFFOLD PROTEIN; MATURATION; ISCU; BIOSYNTHESIS;
D O I：
10.1002/1873-3468.12491
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Iron-sulfur (Fe-S) clusters are ubiquitously conserved and play essential cellular roles. The mechanism of Fe-S cluster biogenesis involves multiple proteins in a complex pathway. Cluster biosynthesis primarily occurs in the mitochondria, but key Fe-S proteins also exist in the cytosol. One such protein, glutaredoxin 3 (Grx3), is involved in iron regulation, sensing, and mediating [2Fe-2S] cluster delivery to cytosolic protein targets, but the cluster donor for cytosolic Grx3 has not been elucidated. Herein, we delineate the kinetic transfer of [2Fe-2S] clusters into Grx3 from potential cytosolic carrier/scaffold proteins, IscU and Nfu, to evaluate a possible model for Grx3 reconstitution in vivo.
引用
收藏
页码：4531 / 4540
页数：10
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