Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10755475 | Biochemical and Biophysical Research Communications | 2014 | 6 Pages |
Abstract
Thymine DNA glycosylase (TDG) is a base excision repair enzyme that interacts with the small ubiquitin-related modifier (SUMO)-targeted ubiquitin E3 ligase RNF4 and functions in the active DNA demethylation pathway. Here we showed that both SUMOylated and non-modified forms of endogenous TDG fluctuated during the cell cycle and in response to drugs that perturbed cell cycle progression, including hydroxyurea and nocodazole. Additionally, we detected a SUMOylation-independent association between TDG and RNF4 in vitro as well as in vivo, and observed that both forms of TDG were efficiently degraded in RNF4-depleted cells when arrested at S phase. Our findings provide insights into the in vivo dynamics of TDG SUMOylation and further clarify the TDG-RNF4 interaction.
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Authors
Taishi Moriyama, Yuka Fujimitsu, Yushi Yoshikai, Takashi Sasano, Koji Yamada, Masataka Murakami, Takeshi Urano, Kaoru Sugasawa, Hisato Saitoh,