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dc.contributor.authorRyu, Hyunju
dc.contributor.authorFuruta, Maiko
dc.contributor.authorKirkpatrick, Donald
dc.contributor.authorGygi, Steven P.
dc.contributor.authorAzuma, Yoshiaki
dc.date.accessioned2014-04-15T18:36:59Z
dc.date.available2014-04-15T18:36:59Z
dc.date.issued2010-11-15
dc.identifier.citationRyu, Hyunju, Maiko Furuta, Donald Kirkpatrick, Steven P. Gygi, and Yoshiaki Azuma. 2010. “PIASy-dependent SUMOylation regulates DNA topoisomerase IIα activity.” J Cell Biol 191:783-794. http://dx.doi.org/10.1083/jcb.201004033
dc.identifier.urihttp://hdl.handle.net/1808/13490
dc.description.abstractDNA topoisomerase IIα (TopoIIα) is an essential chromosome-associated enzyme with activity implicated in the resolution of tangled DNA at centromeres 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 activity. Together, our findings provide evidence for the regulation 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.
dc.description.sponsorshipM. Furuta was supported as a Japan Society for the Promotion of Science Research Fellow in Biomedical and Behavioral Research at the National Institutes of Health. This project was supported in part by a start-up grant from the Department of Molecular Biosciences at the University of Kansas and National Institutes of Health/National Center for Research Resources, Center For Cancer Experimental Therapeutics at the Centers of Biomedical Research Excellence (CCET-COBRE; P20 RR015563), and is currently supported by National Institutes of Health/National Institute of General Medical Sciences grants GM80278 and GM67945 (to S.P. Gygi).
dc.publisherThe Rockerfeller University Press
dc.rightsThis article is distributed under the terms of an Attribution Noncommercial Share Alike No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution Noncommercial Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/
dc.titlePIASy-dependent SUMOylation regulates DNA topoisomerase IIα activity
dc.typeArticle
kusw.kuauthorRyu, Hyunju
kusw.kuauthorFuruta, Maiko
kusw.kuauthorAzuma, Yoshiaki
kusw.kudepartmentDepartment of Molecular Biosciences
kusw.oastatusfullparticipation
dc.identifier.doi10.1083/jcb.201004033
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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This article is distributed under the terms of an Attribution Noncommercial Share Alike No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution Noncommercial Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
Except where otherwise noted, this item's license is described as: This article is distributed under the terms of an Attribution Noncommercial Share Alike No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution Noncommercial Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).