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Characterizing Requirements for Small Ubiquitin-like Modifier (SUMO) Modification and Binding on Base Excision Repair Activity of Thymine-DNA Glycosylase in Vivo.

J Biol Chem.. 2016-04; 
McLaughlin D,Coey CT,Yang WC,Drohat AC,Matunis MJ.
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... The cells were incubated with primary antibody (1:250 rabbit polyclonal anti-FLAG, GenScript, A00170; 1:250 mouse monoclonal anti-SUMO1, 21C7) (25) in TBS-T. After washing with PBS, the cells were incubated with mouse α488 or rabbit α594 Alexa Fluor-conjugated ...

摘要

Thymine-DNA glycosylase (TDG) plays critical roles in DNA base excision repair and DNA demethylation. It has been proposed, based on structural studies and in vitro biochemistry, that sumoylation is required for efficient TDG enzymatic turnover following base excision. However, whether sumoylation is required for TDG activity in vivo has not previously been tested. We have developed an in vivo assay for TDG activity that takes advantage of its recently discovered role in DNA demethylation and selective recognition and repair of 5-carboxylcytosine. Using this assay, we investigated the role of sumoylation in regulating TDG activity through the use of TDG mutants defective for sumoylation and Small Ubiquitin-like... More

关键词

SUMO-interacting motif (SIM); base excision repair (BER); enzyme turnover; small ubiquitin-like modifier (SUMO); sumoylation