In vivo inhibition of trypanosome mitochondrial topoisomerase II: Effects of kinetoplast DNA maxicircles

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dc.creatorShapiro, T.A.
dc.creatorShowalter, F.
dc.date1994-09
dc.date2013-07-03T05:26:01Z
dc.date2013-07-03T05:26:01Z
dc.date.accessioned2026-06-27T16:31:23Z
dc.descriptionKinetoplast DNA, the mitochondrial DNA of trypanosomes, is a topologically complex structure composed of interlocked minicircles and maxicircles. We previously reported that etoposide, a potent inhibitor of topoisomerase II, promotes the cleavage of about 20% of network minicircle DNA (T. A. Shapiro, V. A. Klein, and P. T. Englund, J. Biol. Chem. 264:4173-4178, 1989). We now find that virtually all maxicircles are released from kinetoplast DNA networks after trypanosomes are treated with etoposide. As expected for a topoisomerase II cleavage product, the linearized maxicircles have protein bound to both 5' ends. After etoposide treatment, the residual minicircle catenanes have a sedimentation coefficient which is only 70% that of controls, and by electron microscopy the networks are less compact. Double-size networks, the characteristic dumbbell-shape forms that normally arise in the final stages of network replication, are replaced by aberrant unit-size forms.
dc.identifierhttps://hdl.handle.net/10568/33069
dc.identifier.urihttp://hdl.handle.net/123456789/125302
dc.languageen
dc.publisherInforma UK Limited
dc.rightsLimited Access
dc.sourceMolecular and Cellular Biology;14: 5891-5897
dc.subjecttrypanosome
dc.subjectdna
dc.subjectmitochondria
dc.subjectanimal diseases
dc.subjectcell biology
dc.subjectmolecular biology
dc.titleIn vivo inhibition of trypanosome mitochondrial topoisomerase II: Effects of kinetoplast DNA maxicircles
dc.typeJournal Article

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