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Article

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

Journal of the American Chemical Society - 17 Oct 2018

Nuñez Nicole N, Khuu Cindy, Babu C Satheesan, Bertolani Steve J, Rajavel Anisha N, Spear Jensen E, Armas Jeremy A, Wright Jon D, Siegel Justin B, Lim Carmay, David Sheila S

Abstract excerpt

The DNA base excision repair (BER) glycosylase MUTYH prevents DNA mutations by catalyzing adenine (A) excision from inappropriately formed 8-oxoguanine (8-oxoG):A mismatches. The importance of this mutation suppression activity in tumor suppressor genes is underscored by the association of inherited variants of MUTYH with colorectal polyposis in a hereditary colorectal cancer syndrome known as MUTYH-associated...

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PMID: 30208271
DOI: 10.1021/jacs.8b06923
PMCID: PMC6443246

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Related research

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The Zinc Linchpin Motif in the DNA Repair Glycosylase MUTYH: Identifying the Zn2+ Ligands and Roles in Damage Recognition and Repair.PMID 30208271Read ↗

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

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

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

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

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

Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repair.Semantic proximity Read ↗

Saturation mapping of <i>MUTYH</i> variant effects using DNA repair reportersSemantic proximity Read ↗

Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.Semantic proximity Read ↗

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

Saturation mapping of MUTYH variant effects using DNA repair reporters.Semantic proximity Read ↗

Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repairSemantic proximity Read ↗

Role of MUTYH in human cancer.Semantic proximity Read ↗

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