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pubmed-article:11602253pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:11602253pubmed:pagination239-42lld:pubmed
pubmed-article:11602253pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11602253pubmed:articleTitleMolecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I): identification of topology of binding.lld:pubmed
pubmed-article:11602253pubmed:affiliationDepartment of Medical Biochemistry, Semmelweis University, Budapest, Hungary.lld:pubmed
pubmed-article:11602253pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11602253pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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