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Protein−Protein Interaction of the Human Poly(ADP-ribosyl)transferase Depends on the Functional State of the Enzyme

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Institut für Biochemie, Freie Universität Berlin, Thielallee 63, D-14195 Berlin, Germany
Cite this: Biochemistry 1997, 36, 24, 7297–7304
Publication Date (Web):June 17, 1997
https://doi.org/10.1021/bi962710g
Copyright © 1997 American Chemical Society

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    Abstract

    Poly(ADP-ribosyl)transferase (pADPRT) is a nuclear protein which catalyzes the polymerization of ADP-ribose using NAD+ as substrate, as well as the transfer of ADP-ribose polymers to itself and other protein acceptors. The catalytic activity of pADPRT strictly depends on the presence of DNA single-strand breaks. In this report, protein−protein interaction of pADPRT was found to depend on both the extent of automodification with poly(ADP-ribose) and the presence of DNA. Specific binding of radiolabeled pADPRT to transblotted proteins was first tested in blot overlay experiments. For radiolabeling, use was made of the ability of the enzyme to incorporate [32P]ADP-ribose from [32P]NAD+. Varying the concentration of NAD+, two different forms of automodified pADPRT were obtained:  oligo(ADP-ribosyl)ated pADPRT with less than 20 ADP-ribose units per chain, and poly(ADP-ribosyl)ated pADPRT with polymer lengths of up to 200 ADP-ribose residues. Interaction of these probes with transblotted HeLa nuclear extracts, purified histones, and distinct regions of recombinant pADPRT was investigated. While the oligo(ADP-ribosyl)ated enzyme associated preferentially with transblotted purified histones, or pADPRT present in HeLa nuclear extracts, poly(ADP-ribosyl)ated pADPRT bound to a variety of transblotted proteins in the nuclear extracts. In the presence of DNA, both the oligo- and the poly(ADP-ribosyl)ated enzymes bound to the transblotted recombinant zinc finger domain of pADPRT even at high salt concentrations. In the absence of DNA, the transblotted automodification domain of pADPRT appeared to be the region involved in self-association. In another set of experiments, unmodified or poly(ADP-ribosyl)ated pADPRT was immobilized on Sepharose. Affinity precipitation of recombinant pADPRT domains confirmed the specific interaction of pADPRT with its zinc finger region and the automodification domain, whereas no interaction was observed with the NAD+ binding domain. Affinity precipitation of HeLa nuclear extracts with poly(ADP-ribosyl)ated pADPRT−Sepharose led to the enrichment of a number of proteins, whereas nuclear proteins bound to the unmodified pADPRT−Sepharose in a smaller extent. The results suggest that protein−protein interaction of the human pADPRT is governed by its functional state.

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     This research was supported by grants from the Deutsche Forschungsgemeinschaft (SCHW 532/4-1) and the Studienstiftung des Deutschen Volkes.

    *

     To whom correspondence should be addressed at the Institut für Biochemie, Freie Universität Berlin, Thielallee 63, D-14195 Berlin, Germany. Fax:  +49-30-838 6509. Phone:  +49-30-838 2910. E-mail:  [email protected].

     Abstract published in Advance ACS Abstracts, June 1, 1997.

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