Binding of ATP to Human DNA topoisomerase i resulting in an alteration of conformation and catalytic activity of the enzyme

Jhutlang Hwang, Huî Jye Chen

研究成果: 雜誌貢獻文章同行評審

摘要

Wo have studied the molecular mechanism of A IP-inhibitory effect on the DNA relaxation activity of human DNA topoisomerase I. We have demon si rated that ATP directly and specifically binds to human DNA topoisonierasc I. To address the question whether the DNA relaxation activity of human UNA topoisomerase 1 was allosterically regulated by ATP, We examined the confor [national change of human DNA topoisomerase 1 upon ATP binding. Human !)NA topoisomerase I was incubated with various concentrations of ATP prior ID the treatment by various proteinases, such as trypsin. chymotrypsin. t her molysin. \'K protease, and proleinase K. Our results show that in the presence of ATP. human DNA topoisomerase I becomes resistant towards degradation by trypsin and chymotrypsin, suggesting that the conformation of human DXA lopoisoincrase I becomes alterated upon ATP binding. This observation suggests that DNA topoisomerase I exhibits at least two conformations. Onr con formation is in the form of Topo I-ATP complex, which executes protein kinasc activity, and t lie other is in thr form of Topo [-DNA complex, which executes DNA relaxation activity.

原文英語
期刊FASEB Journal
12
發行號8
出版狀態已發佈 - 1998
對外發佈

ASJC Scopus subject areas

  • 農業與生物科學(雜項)
  • 生物化學、遺傳與分子生物學 (全部)
  • 生物化學
  • 細胞生物學

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