Journal
FEBS LETTERS
Volume 506, Issue 3, Pages 239-242Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)02919-2
Keywords
poly(ADP-ribose) polymerase I; topoisomerase I binding; topoisomerase I regulation by poly(ADP-ribose); polymerase I; binding sited; topology interaction
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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.
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