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

ABSTRACT: 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 polyposis, or MAP. Many of the MAP variants encompass amino acid changes that occur at positions surrounding the two-metal cofactor-binding sites of MUTYH. One of these cofactors, found in nearly all MUTYH orthologs, is a [4Fe-4S]²⁺ cluster coordinated by four Cys residues located in the N-terminal catalytic domain. We recently uncovered a second functionally relevant meta

SUBMITTER: Nunez NN 

PROVIDER: S-EPMC6443246 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature