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Article

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

Nucleic acids research - 9 Jul 2021

Nakamura Teruya, Okabe Kohtaro, Hirayama Shogo, Chirifu Mami, Ikemizu Shinji, Morioka Hiroshi, Nakabeppu Yusaku, Yamagata Yuriko

Abstract excerpt

Mammalian MutY homologue (MUTYH) is an adenine DNA glycosylase that excises adenine inserted opposite 8-oxoguanine (8-oxoG). The inherited variations in human MUTYH gene are known to cause MUTYH-associated polyposis (MAP), which is associated with colorectal cancer. MUTYH is involved in base excision repair (BER) with proliferating cell nuclear antigen (PCNA) in DNA replication, which is unique and critical for...

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Identifiers

PMID: 34142156
DOI: 10.1093/nar/gkab492
PMCID: PMC8266592

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Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.PMID 34142156Read ↗

Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Semantic proximity Read ↗

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

The Zinc Linchpin Motif in the DNA Repair Glycosylase MUTYH: Identifying the Zn2+ Ligands and Roles in Damage Recognition and Repair.Semantic proximity Read ↗

A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions.Semantic proximity Read ↗

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

Role of MUTYH in human cancer.Semantic proximity Read ↗

MUTYH cancer-associated variants within the interdomain connector differentially impact glycosylase activity and cellular DNA repairSemantic proximity Read ↗

MUTYH Cancer-Associated Variants Within the Interdomain Connector Differentially Impact Glycosylase Activity and Cellular DNA Repair.Semantic proximity Read ↗

MUTYH, an adenine DNA glycosylase, mediates p53 tumor suppression via PARP-dependent cell deathSemantic proximity Read ↗

Human MutY Homolog, a DNA Glycosylase Involved in Base Excision Repair, Physically and Functionally Interacts with Mismatch Repair Proteins Human MutS Homolog 2/Human MutS Homolog 6Semantic proximity Read ↗

Structural Connectivity Between the Zinc Linchpin Motif, the [4Fe-4S] cluster, and the active site orchestrates DNA repair in MUTYHSemantic proximity Read ↗

Understanding the role of the Q338H MUTYH variant in oxidative damage repair.Semantic proximity Read ↗

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