PIASy-dependent SUMOylation Regulates DNA Topoisomerase IIα Activity

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PIASy-dependent SUMOylation Regulates DNA Topoisomerase IIα Activity

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Title: PIASy-dependent SUMOylation Regulates DNA Topoisomerase IIα Activity
Author: Ryu, Hyunju; Furuta, Maiko; Kirkpatrick, Donald; Azuma, Yoshiaki; Gygi, Steven P.

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Citation: Ryu, Hyunju, Maiko Furuta, Donald Kirkpatrick, Steven P. Gygi, and Yoshiaki Azuma. 2010. PIASy-dependent SUMOylation regulates DNA topoisomerase IIα activity. The Journal of Cell Biology 191(4): 783-794.
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Abstract: DNA topoisomerase IIα (TopoIIα) is an essential chromosome-associated enzyme with activity im- plicated in the resolution of tangled DNA at cen- tromeres before anaphase onset. However, the regulatory mechanism of TopoIIα activity is not understood. Here, we show that PIASy-mediated small ubiquitin-like modifier 2/3 (SUMO2/3) modification of TopoIIα strongly inhibits TopoIIα decatenation activity. Using mass spectrometry and biochemical analysis, we demonstrate that TopoIIα is SUMOylated at lysine 660 (Lys660), a residue located in the DNA gate domain, where both DNA cleavage and religation take place. Remarkably, loss of SUMOylation on Lys660 eliminates SUMOylation-dependent inhibition of TopoIIα, which indicates that Lys660 SUMOylation is critical for PIASy-mediated inhibition of TopoIIα activ- ity. Together, our findings provide evidence for the reg- ulation of TopoIIα activity on mitotic chromosomes by SUMOylation. Therefore, we propose a novel mechanism for regulation of centromeric DNA catenation during mitosis by PIASy-mediated SUMOylation of TopoIIα.
Published Version: doi://10.1083/jcb.201004033
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2983052/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:5265976
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