Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli

Tatsurou Tajiri, Hisaji Maki, Mutsuo Sekiguchi

Research output: Contribution to journalArticlepeer-review

315 Citations (Scopus)

Abstract

8-Oxo-dGTP (8-oxo-7,8-dihydrodeoxyguanosine triphosphate) is a potent mutagenic substrate for DNA synthesis. The accumulation of 8-oxo-dGTP in the nucleotide pool induces G:C → T:A transversion as well as A:T → C:G transversion, and Escherichia coli cells possess mechanisms for preventing such mutations. The mutT gene product specifically hydrolyzes 8-oxo-dGTP to the monophosphate form while the mutM and the mutY gene products function to correct mispairs caused by incorporation of 8-oxoguanine into DNA. From analyses of forward mutations induced in cells lacking 8-oxo-dGTPase (MutT protein) and/or repair enzymes that suppress mutations caused by 8-oxoguanine in DNA (MutM and MutY proteins), cooperative functions of these proteins in control of the spontaneous mutagenesis became evident. In mutator strains lacking MutT and/or MutM proteins, 8-oxoguanine of DNA increased to a concentration expected from the increased rate of mutation.

Original languageEnglish
Pages (from-to)257-267
Number of pages11
JournalMutation Research-DNA Repair
Volume336
Issue number3
DOIs
Publication statusPublished - May 1995

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Toxicology
  • Genetics

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