Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bpj.2010.07.013
DC FieldValue
dc.titleControl of the flow properties of DNA by topoisomerase II and its targeting inhibitor
dc.contributor.authorKundukad, B.
dc.contributor.authorVan Der Maarel, J.R.C.
dc.date.accessioned2014-10-16T09:19:13Z
dc.date.available2014-10-16T09:19:13Z
dc.date.issued2010
dc.identifier.citationKundukad, B., Van Der Maarel, J.R.C. (2010). Control of the flow properties of DNA by topoisomerase II and its targeting inhibitor. Biophysical Journal 99 (6) : 1906-1915. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bpj.2010.07.013
dc.identifier.issn00063495
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/96078
dc.description.abstractThe flow properties of DNA are important for understanding cell division and, indirectly, cancer therapy. DNA topology controlling enzymes such as topoisomerase II are thought to play an essential role. We report experiments showing how double-strand passage facilitated by topoisomerase II controls DNA rheology. For this purpose, we have measured the elastic storage and viscous loss moduli of a model system comprising bacteriophage λ- DNA and human topoisomerase IIα using video tracking of the Brownian motion of colloidal probe particles. We found that the rheology is critically dependent on the formation of temporal entanglements among the DNA molecules with a relaxation time of ∼1 s. We observed that topoisomerase II effectively removes these entanglements and transforms the solution from an elastic physical gel to a viscous fluid depending on the consumption of ATP. A second aspect of this study is the effect of the generic topoisomerase II inhibitor adenylyl-imido- diphosphate (AMP-PNP). In mixtures of AMP-PNP and ATP, the double-strand passage reaction gets blocked and progressively fewer entanglements are relaxed. A total replacement of ATP by AMP-PNP results in a temporal increase in elasticity at higher frequencies, but no transition to an elastic gel with fixed cross-links. © 2010 by the Biophysical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bpj.2010.07.013
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.description.doi10.1016/j.bpj.2010.07.013
dc.description.sourcetitleBiophysical Journal
dc.description.volume99
dc.description.issue6
dc.description.page1906-1915
dc.description.codenBIOJA
dc.identifier.isiut000282197500028
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