Abstract
The antitumor drug 4'-(9-acridinylamino)methanesulfon-m-anisidide which stimulates the cleavable complex formation between mammalian DNA topoisomerase II and DNA also stimulates the cleavable complex formation between bacteriophage T4-induced DNA topoisomerase and DNA. In the presence of 4'-(9-acridinylamino)methanesulfon-m-anisidide, T4 DNA topoisomerase and DNA for a 'cleavable complex' which is characterized by its sensitivity to protein-denaturant treatment. Upon protein-denaturant treatment, the phosphodiester bond of DNA is cleaved, and the gene 52 protein subunit of the topoisomerase becomes covalently linked to the 5'-end of the broken DNA. The covalent protein-DNA linkage has been determined by both paper electrophoresis and thin layer chromatography to be tyrosyl phosphate.
| Original language | English |
|---|---|
| Pages (from-to) | 9177-9181 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 259 |
| Issue number | 14 |
| Publication status | Published - 1984 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry