Abstract：
:Thymine DNA glycosylase (TDG) is a base excision repair enzyme with key functions in epigenetic regulation. Performing a critical step in a pathway for active DNA demethylation, TDG removes 5-formylcytosine and 5-carboxylcytosine, oxidized derivatives of 5-methylcytosine that are generated by TET (ten-eleven translocation) enzymes. We determined a crystal structure of TDG bound to DNA with a noncleavable (2'-fluoroarabino) analogue of 5-formyldeoxycytidine flipped into its active site, revealing how it recognizes and hydrolytically excises fC. Together with previous structural and biochemical findings, the results illustrate how TDG employs an adaptable active site to excise a broad variety of nucleobases from DNA.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Pidugu LS,Flowers JW,Coey CT,Pozharski E,Greenberg MM,Drohat ACdoi
10.1021/acs.biochem.6b00982subject
Has Abstractpub_date
2016-11-15 00:00:00pages
6205-6208issue
45eissn
0006-2960issn
1520-4995pii
10.1021/acs.biochem.6b00982journal_volume
55pub_type
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