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A Unique ATP-Dependent DNA Topoisomerase from Trypanosomatids

  • Joseph Shlomai
  • Anat Zadok
  • Dale Frank
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 179)

Abstract

Crithidia fasciculata DNA topoisomerase (22) has been purified to near homogeneity from trypanosomatid cell extracts. The purified enzyme catalyzes the reversible interconversion of monomeric duplex DNA circles and catenanes in an ATP dependent reaction. Reversible catenane formation is affected by the ionic strength and is dependent upon the action of a crithidial DNA binding protein, which could be substituted for the polyamine spermidine. Covalently sealed DNA circles are specifically used as substrates for decatenation. Nicking, but not relaxation per se, inhibits network decatenation and has little or no effect on catenane formation. The catalytic properties of this enzyme and its potential role in the prereplication release and post replication reattachment of kDNA minicircles are discussed.

Keywords

Polyamine Spermidine kDNA Minicircles kDNA Network Decatenation Decatenation Decatenation Reaction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Joseph Shlomai
    • 1
  • Anat Zadok
    • 1
  • Dale Frank
    • 1
  1. 1.The Kuvin Centre for the Study of Infectious and Tropical DiseasesThe Hebrew University-Hadassah Medical SchoolJerusalemIsrael

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