Identification of the breakage-reunion subunit of T4 DNA topoisomerase

T. C. Rowe, K. M. Tewey, Leroy-Fong Liu

Research output: Contribution to journalArticlepeer-review

67 Citations (Scopus)

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 languageEnglish
Pages (from-to)9177-9181
Number of pages5
JournalJournal of Biological Chemistry
Volume259
Issue number14
Publication statusPublished - 1984
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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