A DNA oligomer containing 2,2,4-triamino-5(2H)-oxazolone is incised by human NEIL1 and NTH1

Katsuhito Kino, Masashi Takao, Hiroshi Miyazawa, Fumio Hanaoka

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)

Abstract

The nucleobase derivative, 2,2,4-triamino-5(2. H)-oxazolone (Oz), is an oxidation product of guanine or of 8-oxo-7,8-dihydroguanine that causes G-to-C transversions in DNA. Human NEIL1 (hNEIL1) and NTH1 (hNTH1) are homologues of two prokaryotic base excision repair enzymes, FPG/NEI and NTH, respectively. Here, we demonstrated that hNEIL1 and hNTH1 cleave Oz sites as efficiently as 5-hydroxyuracil sites. Thus, hNEIL1 and hNTH1 can repair Oz lesions. Furthermore, the nicking activities of these enzymes are largely independent of nucleobases opposite Oz; this finding indicates that removing Oz from Oz:G and Oz:A base pairs might cause an increase in the rate of point mutations in human cells.

Original languageEnglish
Pages (from-to)73-77
Number of pages5
JournalMutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
Volume734
Issue number1-2
DOIs
Publication statusPublished - 2012 Jun 1

Keywords

  • Base excision repair enzyme
  • Guanine oxidation
  • Human NEIL1
  • Human NTH1
  • Oxazolone

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Health, Toxicology and Mutagenesis

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