Unit

UNIT 3.9 DNA Repair Enzymes

  1. Thomas C. Evans,
  2. Nicole M. Nichols

Published Online: 1 OCT 2008

DOI: 10.1002/0471142727.mb0309s84

Current Protocols in Molecular Biology

Current Protocols in Molecular Biology

How to Cite

Evans, T. C. and Nichols, N. M. 2008. DNA Repair Enzymes. Current Protocols in Molecular Biology. 84:III:3.9:3.9.1–3.9.12.

Author Information

  1. New England Biolabs, Ipswich, Massachusetts

Publication History

  1. Published Online: 1 OCT 2008
  2. Published Print: OCT 2008

Abstract

In vivo DNA damage impacts the genetic stability of an organism; therefore, multiple pathways utilizing a large number of enzymes have evolved to repair DNA damage. This unit focuses on enzymes involved in base excision repair (BER). The BER enzymes possessing N-glycosylase activity can find and remove a wide variety of damaged bases in a sea of normal bases. The combination of unique substrate specificity, accuracy, and robust in vitro activity of many of these enzymes has led to their use in various experimental techniques, including site-specific DNA cleavage. The enzymes described in this unit are active on many substrates including oxidized purines and pyrimidines, alkylated bases, abasic sites, pyrimidine dimers, deaminated cytosines, and deaminated adenines. Curr. Protoc. Mol. Biol. 84:3.9.1-3.9.12. © 2008 by John Wiley & Sons, Inc.

Keywords:

  • DNA repair;
  • N-glycosylase;
  • COMET assay;
  • UDG;
  • FPG;
  • base excision repair