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

被引:38
作者
Bauer, PI
Chen, HJ
Kenesi, E
Kenessey, I
Buki, KG
Kirsten, E
Hakam, A
Hwang, JI
Kun, E [1 ]
机构
[1] Univ Calif San Francisco, Dept Anat & Cellular & Mol Pharmacol, San Francisco, CA 94143 USA
[2] Semmelweis Univ, Dept Med Biochem, H-1085 Budapest, Hungary
[3] Taipei Univ, Dept Mol Biol, Taipei, Taiwan
基金
匈牙利科学研究基金会;
关键词
poly(ADP-ribose) polymerase I; topoisomerase I binding; topoisomerase I regulation by poly(ADP-ribose); polymerase I; binding sited; topology interaction;
D O I
10.1016/S0014-5793(01)02919-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:239 / 242
页数:4
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