Submitted by alp2017 on April 24, 2015 - 10:48am
| Title | Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine. |
| Publication Type | Journal Article |
| Year of Publication | 1986 |
| Authors | Brougham MJ, Rowe TC, Holloman WK |
| Journal | Biochemistry |
| Volume | 25 |
| Issue | 23 |
| Pagination | 7362-8 |
| Date Published | 1986 Nov 18 |
| ISSN | 0006-2960 |
| Keywords | Basidiomycota, Binding Sites, DNA Topoisomerases, Type I, DNA, Single-Stranded, Kinetics, Protein Binding, Substrate Specificity, Tyrosine, Ustilago |
| Abstract | Highly purified topoisomerase from Ustilago breaks single-stranded DNA, forming a complex with protein covalently bound to the DNA. Methods used to detect the complexes include a nitrocellulose filter assay, electrophoresis of the DNA-protein complex in agarose gels containing alkali, and isolation of the complex after removal of all but a small oligonucleotide fragment bound to the protein. The linkage of the Ustilago topoisomerase is to the 3' end of the broken strand of DNA. The DNA-protein complex formed is through a phosphodiester bond to tyrosine. |
| Alternate Journal | Biochemistry |
| PubMed ID | 3026452 |
| Grant List | GM-27103 / GM / NIGMS NIH HHS / United States GM-36327 / GM / NIGMS NIH HHS / United States |