Uracil-DNA glycosylases-Structural and functional perspectives on an essential family of DNA repair enzymes

被引:149
作者
Schormann, N. [1 ]
Ricciardi, R. [2 ]
Chattopadhyay, D. [1 ]
机构
[1] Univ Alabama Birmingham, Dept Med, Birmingham, AL 35294 USA
[2] Univ Penn, Sch Dent Med, Dept Microbiol, Abramson Canc Ctr, Philadelphia, PA 19104 USA
关键词
DNA repair; uracil-DNA glycosylase; base excision repair; DNA mimicry; BASE-EXCISION-REPAIR; SINGLE-STRANDED-DNA; ESCHERICHIA-COLI; VACCINIA-VIRUS; CRYSTAL-STRUCTURE; DAMAGE RECOGNITION; INHIBITOR PROTEIN; POLYMERASE-BETA; SUBSTRATE-SPECIFICITY; MUTATIONAL ANALYSIS;
D O I
10.1002/pro.2554
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
Uracil-DNA glycosylases (UDGs) are evolutionarily conserved DNA repair enzymes that initiate the base excision repair pathway and remove uracil from DNA. The UDG superfamily is classified into six families based on their substrate specificity. This review focuses on the family I enzymes since these are the most extensively studied members of the superfamily. The structural basis for substrate specificity and base recognition as well as for DNA binding, nucleotide flipping and catalytic mechanism is discussed in detail. Other topics include the mechanism of lesion search and molecular mimicry through interaction with uracil-DNA glycosylase inhibitors. The latest studies and findings detailing structure and function in the UDG superfamily are presented. ;
引用
收藏
页码:1667 / 1685
页数:19
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