E2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex

Christopher T. Coey, Megan E. Fitzgerald, Atanu Maiti, Katherine H. Reiter, Catherine M. Guzzo, Michael J. Matunis, Alexander C. Drohat

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Background: Post-translational SUMO modification of TDG weakens its DNA binding and was proposed to regulate dissociation of a tight enzyme-product complex. Results: In vitro sumoylation of TDG by SUMO-1 and SUMO-2 is efficient for free and DNA-bound TDG. Conclusion: E2-mediated sumoylation is not selective for product-bound TDG but could potentially stimulate product release. Significance: Our findings inform the mechanism and role of TDG sumoylation.

Original languageEnglish (US)
Pages (from-to)15810-15819
Number of pages10
JournalJournal of Biological Chemistry
Volume289
Issue number22
DOIs
StatePublished - May 30 2014

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