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J. Biol. Chem., Vol. 256, Issue 20, 10354-10361, 10, 1981

Purification and properties of a topoisomerase from Ustilago maydis

TC Rowe, JR Rusche, MJ Brougham and WK Holloman

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.
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