A unique ATP-dependent DNA topoisomerase from trypanosomatids.

J. Shlomai; A. Zadok; D. Frank

doi:10.1007/978-1-4684-8730-5_42

A unique ATP-dependent DNA topoisomerase from trypanosomatids.

J. Shlomai^*
, A. Zadok
, D. Frank

^*Corresponding author for this work

Institute for Medical Research Israel-Canada (IMRIC)

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

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.

Original language	English
Pages (from-to)	409-422
Number of pages	14
Journal	Advances in Experimental Medicine and Biology
Volume	179
DOIs	https://doi.org/10.1007/978-1-4684-8730-5_42
State	Published - 1984

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10.1007/978-1-4684-8730-5_42

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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.",

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N2 - 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.

AB - 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.

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A unique ATP-dependent DNA topoisomerase from trypanosomatids.

Abstract

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