Purification and properties of a topoisomerase from Ustilago maydis [Fungus]

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...

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Published inThe Journal of biological chemistry Vol. 256; no. 20; pp. 10354 - 10361
Main Authors Rowe, T.C, Rusche, J.R, Brougham, M.J, Hollomann, W.K
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 25.10.1981
Subjects
Anti-Bacterial Agents - pharmacology
Basidiomycota - enzymology
DNA topoisomerase
DNA Topoisomerases, Type I - isolation & purification
DNA Topoisomerases, Type I - metabolism
Enzyme Activation
Histones - pharmacology
Kinetics
Magnesium - pharmacology
Molecular Weight
Polynucleotides - pharmacology
purification
Ribonucleotides - pharmacology
topoisomerase
Ustilago - enzymology
Ustilago maydis
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Summary: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.
Bibliography:F60
8137244
H20
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)68626-6