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blm and rmi1 alleviate rpa inhibition of topoiiiα decatenase activityblm rmi1缓解则抑制topoiiiαdecatenase活动.pdf

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blm and rmi1 alleviate rpa inhibition of topoiiiα decatenase activityblm rmi1缓解则抑制topoiiiαdecatenase活动

BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity 1 2 2,3 1 Jay Yang , Csanad Z. Bachrati , Ian D. Hickson , Grant W. Brown * 1 Department of Biochemistry and Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario, Canada, 2 Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, United Kingdom, 3 Center for Healthy Aging, Department of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen, Denmark Abstract RPA is a single-stranded DNA binding protein that physically associates with the BLM complex. RPA stimulates BLM helicase activity as well as the double Holliday junction dissolution activity of the BLM-topoisomerase IIIa complex. We investigated the effect of RPA on the ssDNA decatenase activity of topoisomerase IIIa. We found that RPA and other ssDNA binding proteins inhibit decatenation by topoisomerase IIIa. Complex formation between BLM, TopoIIIa, and RMI1 ablates inhibition of decatenation by ssDNA binding proteins. Together, these data indicate that inhibition by RPA does not involve species- specific interactions between RPA and BLM-TopoIIIa-RMI1, which contrasts with RPA modulation of double Holliday junction dissolution. We propose that topoisomerase IIIa and RPA compete to bind to single-stranded regions of catenanes. Interactions with BLM and RMI1 enhance toposiomerase IIIa activity, promoting decatenation in the presence of RPA. Citation: Yang J, Bachrati CZ, Hickson ID, Brown GW (2012) BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity. PLoS ONE 7(7): e41208. doi:10.1371/journal.pone.0041208 Editor: Sergey Korolev, Saint Louis University, United Sta