Crystallizing thoughts about DNA base excision repair

Thomas Hollis, Albert Lau, Tom Ellenberger

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Chemically damaged bases are removed from DNA by glycosylases that locate the damage and cleave the bond between the modified base and the deoxyribose sugar of the DNA backbone. The detection of damaged bases in DNA poses two problems: (1) The aberrant bases are mostly buried within the double helix, and (2) a wide variety of chemically different modifications must be efficiently recognized and removed. The human alkyladenine glycosylase (AAG) and Escherichia coli AlkA DNA glycosylases excise many different types of alkylated bases from DNA. Crystal structures of these enzymes show how substrate bases are exposed to the enzyme active site and they suggest mechanisms of catalytic specificity. Both enzymes bend DNA and flip substrate bases out of the double helix and into the enzyme active site for cleavage. Although AAG and AlkA have very different overall folds, some common features of their substrate-binding sites suggest related strategies for the selective recognition of a chemically diverse group of alkylated substrates.

Original languageEnglish (US)
Title of host publicationBase Excesion Repair
Pages305-314
Number of pages10
StatePublished - Dec 1 2001
Externally publishedYes

Publication series

NameProgress in Nucleic Acid Research and Molecular Biology
Volume68
ISSN (Print)0079-6603

ASJC Scopus subject areas

  • Molecular Biology

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