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Poly(ADP-ribose) catabolism in mammalian cells |
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| Authors: | Jean Lagueux Girish M Shah Luc Ménard Hélène Thomassin Caroline Duchaine Christoph Hengartner Guy G Poirier |
| Institution: | (1) Poly(ADP-ribose) metabolism group, Molecular Endocrinology Research Center, CHUL Research Center, 2705 blvd, Laurier, G1V 4G2 Ste-Foy, Québec, Canada;(2) Present address: Duke University Medical Center, 254 Jones Building Research Drive, Box 3680, 27710 Durham, NC, USA;(3) Present address: Centre de recherche sur l'endocrinologie moléculaire et le développement, CNRS, 9 rue Jules Hetzel, 92190 Meudon-Bellevue, France;(4) Present address: Nine Cambridge Center, Whitehead Institute for Biomedical Research, 02142, MA, USA |
| Abstract: | Poly(ADP-ribose) catabolism is a complex situation involving many proteins and DNA. We have developed anin vitro turnover system where poly(ADP-ribose) metabolism is monitored in presence of different relative amounts of two principal enzymes poly(ADP-ribose) transferase and poly(ADP-ribose) glycohydrolase along with other proteins and DNA. Our current results reviewed here show that the quality of polymer, i.e. chain length and complexity, as well as preference for the nuclear substrate varies depending upon the availability of poly(ADP-ribose) glycohydrolase. These results are interpreted in the light of the recent data implicating poly(ADP-ribose) metabolism in DNA-repair. (Mol Cell Biochem 138: 45–52 1994) |
| Keywords: | poly (ADP-ribose) metabolism turnover chromatin DNA-repair histones |
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