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Purification and properties of a topoisomerase from Ustilago maydis.

Authors :
Rowe TC
Rusche JR
Brougham MJ
Holloman WK
Source :
The Journal of biological chemistry [J Biol Chem] 1981 Oct 25; Vol. 256 (20), pp. 10354-61.
Publication Year :
1981

Abstract

The lower eukaryote Ustilago maydis contains a topoisomerase that removes supercoils from negative and positive superhelical DNA. The enzyme may be a multimeric protein or an aggregate of polypeptides with a native molecular weight of 270,000 as estimated by gel filtration. No cofactors are required by the enzyme, but activity is enhanced by Mg2+. Dependence of activity upon enzyme concentration is not linear. Below a threshold level where topoisomerase cannot ordinarily be detected, addition of H1 histone sharply stimulates activity. ATP and a number of structural analogues inhibit the enzyme.

Details

Language :
English
ISSN :
0021-9258
Volume :
256
Issue :
20
Database :
MEDLINE
Journal :
The Journal of biological chemistry
Publication Type :
Academic Journal
Accession number :
6270108