Submitted by alp2017 on April 24, 2015 - 11:31am
| Title | Purification and properties of a topoisomerase from Ustilago maydis. |
| Publication Type | Journal Article |
| Year of Publication | 1981 |
| Authors | Rowe TC, Rusche JR, Brougham MJ, Holloman WK |
| Journal | J Biol Chem |
| Volume | 256 |
| Issue | 20 |
| Pagination | 10354-61 |
| Date Published | 1981 Oct 25 |
| ISSN | 0021-9258 |
| Keywords | Anti-Bacterial Agents, Basidiomycota, DNA Topoisomerases, Type I, Enzyme Activation, Histones, Kinetics, Magnesium, Molecular Weight, Polynucleotides, Ribonucleotides, Ustilago |
| 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. |
| Alternate Journal | J. Biol. Chem. |
| PubMed ID | 6270108 |
| Grant List | GM 27103 / GM / NIGMS NIH HHS / United States |