DNA Repair Enzymes

Thomas C. Evans1, Nicole M. Nichols1

1 New England Biolabs, Ipswich, Massachusetts
Publication Name:  Current Protocols in Molecular Biology
Unit Number:  Unit 3.9
DOI:  10.1002/0471142727.mb0309s84
Online Posting Date:  October, 2008
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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

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Table of Contents

  • Introduction
  • Enzyme: Escherichia coli Uracil DNA Glycosylase
  • Enzyme: Archaeoglobus fulgidis Uracil DNA Glycosylase
  • Enzyme: Escherichia coli MutY
  • Enzyme: Human Alkyladenine‐DNA Glycosylase
  • Enzyme: Escherichia coli Formamidopyrimidine [fapy]‐DNA Glycosylase
  • Enzyme: Escherichia coli Endonuclease III
  • Enzyme: Eschericia Coli Endonuclease VIII
  • Enzyme: Human 8‐Oxoguanine DNA Glycosylase
  • Enzyme: T4 Pyrimidine Dimer Glycosylase
  • Enzyme: Escherichia coli Endonuclease IV
  • Enzyme: Human Apurinic/Apyrimidinic Endonuclease I
  • Enzyme: Esherichia Coli Endonuclease V
  • Multi‐Enzyme DNA Repair
  • Literature Cited
  • Figures
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Literature Cited

Literature Cited
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