Abstract
The primary protein target for poly(ADP-ribose) modification in mammalian chromatin is poly(ADP-ribose)polymerase (PADPRP) itself (1,2). However, our current understanding of this reaction at the biochemical level is very limited. Here, we have utilized 2’ and 3’-deoxyNAD analogs as substrates for the amino acid-specific covalent modification of PADPRP with monomers and polymers of ADP-ribose. Specific mono(ADP-ribosyl)ation of PADPRP at arginine residues was achieved by incubating pure polymerase with mono(ADP-ribosyl)transferase A (3) from turkey erythrocytes and 2’-deoxyNAD as an ADP-ribosylation substrate (4,5). In contrast, the auto[poly(ADP-ribosyl)ation] of PADPRP was performed with 3’-deoxyNAD. Utilization of this NAD analog is advantageous because it does not alter the physicochemical properties of the polymerase upon modification (6,7).
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© 1992 Springer Science+Business Media New York
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Martinez-Cadena, M.G., Pedraza-Reyes, M., Alvarez-Gonzalez, R. (1992). Amino Acid Specific Modification of Poly(ADP-ribose)polymerase with Monomers and Polymers of ADP-ribose. In: Poirier, G.G., Moreau, P. (eds) ADP-Ribosylation Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-8718-1_53
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DOI: https://doi.org/10.1007/978-1-4419-8718-1_53
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