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Article

The C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities.

Nucleic acids research - 15 Jun 2003

Li Lina, Lu A-Lien

Abstract excerpt

Escherichia coli MutY is an adenine and a weak guanine DNA glycosylase involved in reducing mutagenic effects of 7,8-dihydro-8-oxo-guanine (8-oxoG). The C-terminal domain of MutY is required for 8-oxoG recognition and is critical for mutation avoidance of oxidative damage. To determine which residues of this domain are involved in 8-oxoG recognition, we constructed four MutY mutants based on similarities to MutT,...

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Identifiers

PMID: 12799430
DOI: 10.1093/nar/gkg434
PMCID: PMC162338

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities.PMID 12799430Read ↗

The C-terminal domain of MutY glycosylase determines the 7,8-dihydro-8-oxo-guanine specificity and is crucial for mutation avoidance.Semantic proximity Read ↗

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Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe.Semantic proximity Read ↗

Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase.Semantic proximity Read ↗

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The mutT defect does not elevate chromosomal fragmentation in Escherichia coli because of the surprisingly low levels of MutM/MutY-recognized DNA modifications.Semantic proximity Read ↗

MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNASemantic proximity Read ↗

Fission yeast (Schizosaccharomyces pombe) cells defective in the MutY-homologous glycosylase activity have a mutator phenotype and are sensitive to hydrogen peroxide.Semantic proximity Read ↗

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