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Purification and properties of a topoisomerase from Ustilago maydis.
- 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.
- Subjects :
- Anti-Bacterial Agents pharmacology
DNA Topoisomerases, Type I metabolism
Enzyme Activation
Histones pharmacology
Kinetics
Magnesium pharmacology
Molecular Weight
Polynucleotides pharmacology
Ribonucleotides pharmacology
Basidiomycota enzymology
DNA Topoisomerases, Type I isolation & purification
Ustilago enzymology
Subjects
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