InterPro domain: IPR044298

This family includes DNA glycosylases involved in DNA damage repair, including Adenine-DNA glycosylase MutY and its homologues (MutYH) and Thymine-DNA glycosylase MIG. MutY plays an important role in the prevention of DNA mutations resulting from the presence of the oxidatively damaged lesion 7,8-dihydro-8-oxo-2'-deoxyguanosine (8-OxoG). 8-OxoG can mispair with 2'-deoxycytidine 5'-triphosphate or with 2'-deoxyadenosine triphosphate during DNA replication, forming C*8-oxoG and A*8-oxoG mispairs. If unrepaired, the A=8-oxoG mispairs can result in deleterious C:G to A:T transversions. MutY, with its DNA glycosylase activity, excises adenine paired with guanine or 8-oxoG [ 1 ]. Mutations in this enzyme cause MUTYH-associated polyposis (MAP) which results in the accumulation of G:T mismatched DNA caused by oxidative damage [ 2 ]. MIG excises thymine from T/G mismatches and it also has a weak DNA glycosylase activity on uracil paired with various bases [ 3 ].

1. Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. U.S.A. 86, 8877-81
2. Functional Complementation Assay for 47 MUTYH Variants in a MutY-Disrupted Escherichia coli Strain. Hum Mutat 36, 704-11
3. Expression and characterization of thymine-DNA glycosylase from Aeropyrum pernix. Protein Expr Purif 70, 1-6