Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An Escherichia coli MutY mutant without the six-helix barrel domain is a dimer in solution and assembles cooperatively into multisubunit complexes with DNA.

The Journal of biological chemistry - 10 Dec 2004

Lee Chih-Yung, Bai Haibo, Houle Rebecca, Wilson Gerald M, Lu A-Lien

Abstract excerpt

Escherichia coli MutY is an adenine and weak guanine DNA glycosylase involved in reducing the mutagenic effects of 7,8-dihydro-8-oxoguanine (GO). MutY contains three structural domains: an iron-sulfur module, a six-helix barrel module with the helix-hairpin-helix motif, and a C-terminal domain. Here, we demonstrate that the mutant MutY(Delta26-134), which lacks the six-helix barrel domain, cannot complement the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Dimerization
Share to DNA Glycosylases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genes, Bacterial

Share to Genetic Complementation Test

Share to Macromolecular Substances

Share to Protein Structure, Quaternary

Share to Sequence Deletion

Share to Solutions

Source

Identifiers

PMID: 15456766
DOI: 10.1074/jbc.M405271200

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An Escherichia coli MutY mutant without the six-helix barrel domain is a dimer in solution and assembles cooperatively into multisubunit complexes with DNA.PMID 15456766Read ↗

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

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 ↗

Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA.Semantic proximity Read ↗

Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.Semantic proximity Read ↗

Characterization of an Escherichia coli mutant MutY with a cysteine to alanine mutation at the iron-sulfur cluster domain.Semantic proximity Read ↗

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

Physical and functional interactions between Escherichia coli MutY glycosylase and mismatch repair protein MutS.Semantic proximity Read ↗

MutY and MutY homologs (MYH) in genome maintenance.Semantic proximity Read ↗

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

Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine:guanine mispair to prevent spontaneous G:C-->C:G transversions.Semantic proximity Read ↗

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 ↗

Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.