Repair of 8-hydroxyguanine in DNA by mammalian N-methylpurine-DNA glycosylase

Tadayoshi Bessho, Rabindra Roy, Kazuo Yamamoto, Hiroshi Kasai, Susumu Nishimura, Keizo Tano, Sankar Mitra

Research output: Contribution to journalArticle

135 Scopus citations

Abstract

8-Hydroxyguanine is one of the major base lesions implicated in mutagenesis induced by ionizing radiation and radiomimetic agents. This lesion appears to be repaired by human cells via multiple pathways including the one that involves a base glycosylase. Mouse N-methylpurine-DNA glycosylase, responsible for the removal of N-alkylpurines in DNA that are induced by simple monofunctional alkylating agents, also releases 8-hydroxyguanine from DNA in vitro and in vivo in Escherichia coli. The human N-methylpurine-DNA glycosylase, with a lower preference for N-alkylguanine than the mouse protein, removes the oxidized base less efficiently than the mouse protein. The recombinant mammalian glycosylases can rescue E. coli lacking MutM (Fpg) protein, the DNA glycosylase that is primarily responsible for removing 8-hydroxyguanine from the bacterial DNA.

Original languageEnglish (US)
Pages (from-to)8901-8904
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number19
DOIs
StatePublished - Oct 1 1993

Keywords

  • DNA repair
  • Mutation suppression
  • Oxidative DNA damage

ASJC Scopus subject areas

  • General

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