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Cited by 37DNA Repair MechanismsDNA and Nucleic Acid ChemistryEnzyme Structure and Function

Investigations of pyrimidine dimer glycosylases—A paradigm for DNA base excision repair enzymology

Lloyd, R. Stephen·2005·Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
DOI 10.1016/j.mrfmmm.2005.04.003
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Abstract

The most prevalent forms of cancer in humans are the non-melanoma skin cancers, with over a million new cases diagnosed in the United States annually. The portions of the body where these cancers arise are almost exclusively on the most heavily sun-exposed tissues. It is now well established that exposure to ultraviolet light (UV) causes not only damage to DNA that subsequently generates mutations and a transformed phenotype, but also UV-induced immunosuppression. Human cells have only one mechanism to remove the UV-induced dipyrimidine DNA photoproducts: nucleotide excision repair (NER). However, simpler organisms such as bacteria, bacteriophages and some eukaryotic viruses contain up to three distinct mechanisms to initiate the repair of UV-induced dipyrimidine adducts: NER, base excision repair (BER) and photoreversal. This review will focus on the biology and the mechanisms of DNA glycosylase/AP lyases that initiate BER of cis-syn cyclobutane pyrimidine dimers. One of these enzymes, the T4 pyrimidine dimer glycosylase (T4-pdg), formerly known as T4 endonuclease V has served as a model in the study of this entire class of enzymes. It was the first DNA repair enzyme: (1) for which a biologically significant processive nicking activity was demonstrated; (2) to have its active site determined, (3) to have its crystal structure solved, (4) to be shown to carry out nucleotide flipping, and (5) to be used in human clinical trials for disease prevention.

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Authors
Lloyd, R. S.
Affiliations
Oregon Health & Science University (US)
Corresponding author
Lloyd, R. Stephen
ORCID
Lloyd, R. Stephen
Venue
Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
Publisher
Elsevier BV
Published
2005-09
Volume
577
Issue
1-2
Pages
77-91
ISSN
  • 0027-5107 (ISSN-L)
  • 1386-1964
DOI
10.1016/j.mrfmmm.2005.04.003
OpenAlex
W2077403011
Cited by
37
References
89
Citations by year
2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 1 · 2018: 2 · 2016: 1 · 2012: 2
FWCI
0.27
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Mutation research. Fundamental and molecular mechanisms of mutagenesis (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institutes of Health (ES04091)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
base excision repair, T4 endonuclease V, DNA glycosylase, AP lyase, UV-induced DNA damage, nucleotide excision repair, photoreversal, non-melanoma skin cancer, nucleotide flipping, active site, crystal structure
MeSH terms
Base Sequence, Binding Sites, DNA Repair, Models, Molecular, Dimerization, DNA Glycosylases

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