DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster

被引：107

作者：

Wu, Yuliang ^{[1
]}

Brosh, Robert M., Jr. ^{[2
]}

机构：

[1] Univ Saskatchewan, Dept Biochem, Saskatoon, SK S7N 5E5, Canada

[2] NIA, Lab Mol Gerontol, NIH, NIH Biomed Res Ctr, Baltimore, MD 21224 USA

来源：

NUCLEIC ACIDS RESEARCH | 2012年 / 40卷 / 10期

基金：

美国国家卫生研究院;

关键词：

REPLICATION PROTEIN-A; BASE EXCISION-REPAIR; ANEMIA GROUP J; FANCJ HELICASE; SACCHAROMYCES-CEREVISIAE; XERODERMA-PIGMENTOSUM; GENOME INSTABILITY; ENDONUCLEASE-III; CHARGE-TRANSPORT; STRUCTURAL BASIS;

D O I：

10.1093/nar/gks039

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：

Conserved Iron-Sulfur (Fe-S) clusters are found in a growing family of metalloproteins that are implicated in prokaryotic and eukaryotic DNA replication and repair. Among these are DNA helicase and helicase-nuclease enzymes that preserve chromosomal stability and are genetically linked to diseases characterized by DNA repair defects and/or a poor response to replication stress. Insight to the structural and functional importance of the conserved Fe-S domain in DNA helicases has been gleaned from structural studies of the purified proteins and characterization of Fe-S cluster site-directed mutants. In this review, we will provide a current perspective of what is known about the Fe-S cluster helicases, with an emphasis on how the conserved redox active domain may facilitate mechanistic aspects of helicase function. We will discuss testable models for how the conserved Fe-S cluster might operate in helicase and helicase-nuclease enzymes to conduct their specialized functions that help to preserve the integrity of the genome.

引用

页码：4247 / 4260

页数：14

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