Molecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I): Identification of topology of binding

Pal I. Bauer, Hui Je Chen, Erzsebet Kenesi, Istvan Kenessey, Kalman G. Buki, Eva Kirsten, Alaeddin Hakam, Jaulang I. Hwang, Ernest Kun

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43 引文 斯高帕斯(Scopus)

摘要

The molecular interactions of poly(ADP-ribose) polymerase I (PARP I) and topoisomerase I (Topo I) have been determined by the analysis of physical binding of the two proteins and some of their polypeptide components and by the effect of PARP I on the enzymatic catalysis of Topo I. Direct association of Topo I and PARP I as well as the binding of two Topo I polypeptides to PARP I are demonstrated. The effect of PARP I on the 'global' Topo I reaction (scission and religation), and the activation of Topo I by the 36 kDa polypeptide of PARP I and catalytic modifications by poly(ADP-ribosyl)ation are also shown. The covalent binding of Topo I to circular DNA is activated by PARP I similar to the degree of activation of the 'global' Topo I reaction, whereas the religation of DNA is unaffected by PARP I. The geometry of PARP I-Topo I interaction compared to automodified PARP I was reconstructed from direct binding assays between glutathione S-transferase fusion polypeptides of Topo I and PARP I demonstrating highly selective binding, which was correlated with amino acid sequences and with the 'C clamp' model derived from X-ray crystallography.

原文英語
頁(從 - 到)239-242
頁數4
期刊FEBS Letters
506
發行號3
DOIs
出版狀態已發佈 - 十月 12 2001

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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