A unique ATP-dependent DNA topoisomerase from trypanosomatids.

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.

journal_name

Adv Exp Med Biol

authors

Shlomai J,Zadok A,Frank D

doi

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

subject

Has Abstract

pub_date

1984-01-01 00:00:00

pages

409-22

eissn

0065-2598

issn

2214-8019

journal_volume

179

pub_type

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