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

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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Thymine DNA Glycosylase
Sumoylation
Ubiquitin
Enzymes
DNA

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

E2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex. / Coey, Christopher T.; Fitzgerald, Megan E.; Maiti, Atanu; Reiter, Katherine H.; Guzzo, Catherine M.; Matunis, Michael J; Drohat, Alexander C.

In: Journal of Biological Chemistry, Vol. 289, No. 22, 30.05.2014, p. 15810-15819.

Research output: Contribution to journalArticle

Coey, Christopher T. ; Fitzgerald, Megan E. ; Maiti, Atanu ; Reiter, Katherine H. ; Guzzo, Catherine M. ; Matunis, Michael J ; Drohat, Alexander C. / E2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex. In: Journal of Biological Chemistry. 2014 ; Vol. 289, No. 22. pp. 15810-15819.
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