TY - JOUR
T1 - E2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex
AU - Coey, Christopher T.
AU - Fitzgerald, Megan E.
AU - Maiti, Atanu
AU - Reiter, Katherine H.
AU - Guzzo, Catherine M.
AU - Matunis, Michael J.
AU - Drohat, Alexander C.
PY - 2014/5/30
Y1 - 2014/5/30
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M114.572081
DO - 10.1074/jbc.M114.572081
M3 - Article
C2 - 24753249
AN - SCOPUS:84901705539
SN - 0021-9258
VL - 289
SP - 15810
EP - 15819
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 22
ER -