Purification and properties of a topoisomerase from Ustilago maydis.

TitlePurification and properties of a topoisomerase from Ustilago maydis.
Publication TypeJournal Article
Year of Publication1981
AuthorsRowe TC, Rusche JR, Brougham MJ, Holloman WK
JournalJ Biol Chem
Date Published1981 Oct 25
KeywordsAnti-Bacterial Agents, Basidiomycota, DNA Topoisomerases, Type I, Enzyme Activation, Histones, Kinetics, Magnesium, Molecular Weight, Polynucleotides, Ribonucleotides, Ustilago

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.

Alternate JournalJ. Biol. Chem.
PubMed ID6270108
Grant ListGM 27103 / GM / NIGMS NIH HHS / United States

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