The role of chaperones in iron-sulfur cluster biogenesis

被引:23
作者
Puglisi, Rita [1 ,2 ]
Pastore, Annalisa [1 ,2 ,3 ]
机构
[1] Kings Coll London, UK Dementia Res Inst, London SE5 9RT, England
[2] Kings Coll London, Wohl Inst, London, England
[3] Univ Pavia, Dept Mol Med, Pavia, Italy
来源
FEBS LETTERS | 2018年 / 592卷 / 24期
基金
英国生物技术与生命科学研究理事会;
关键词
Chaperones; iron-sulfur cluster; neurodegeneration; protein folding; structural biology; ASSEMBLY PROTEIN ISCU; FE-S PROTEINS; MOLECULAR CHAPERONES; SCAFFOLD PROTEIN; SUBSTRATE-BINDING; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; HSP70; CHAPERONES; HSCB; BIOSYNTHESIS;
D O I
10.1002/1873-3468.13245
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 cluster biogenesis is a complex process mediated by numerous proteins among which two from bacteria chaperones, called HscB and HscA in bacteria. They are highly conserved up to eukaryotes and homologous to DnaJ and DnaK, respectively, but with specific differences. As compared with other chaperones, HscB and HscA have escaped attention and relatively little is known about their functions. After briefly introducing the various chaperone families, we reviewed here the current structural and functional knowledge HscA and HscB and on their role in cluster formation. We critically evaluated the literature and highlighted the weak aspects which will require more attention in the future. We sincerely hope that this study will inspire new interest on this important and interesting system.
引用
收藏
页码:4011 / 4019
页数:9
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