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Isabelle M, Moreel X, Gagné JP, et al. Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry. Proteome Sci. 2010;8:22doi: 10.1186/1477-5956-8-22.
Isabelle, M., Moreel, X., Gagné, J. P., Rouleau, M., Ethier, C., Gagné, P., Hendzel, M. J., & Poirier, G. G. (2010). Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry. Proteome science, 822. https://doi.org/10.1186/1477-5956-8-22
Isabelle, Maxim, et al. "Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry." Proteome science vol. 8 (2010): 22. doi: https://doi.org/10.1186/1477-5956-8-22
Isabelle M, Moreel X, Gagné JP, Rouleau M, Ethier C, Gagné P, Hendzel MJ, Poirier GG. Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry. Proteome Sci. 2010 Apr 13;8:22. doi: 10.1186/1477-5956-8-22. PMID: 20388209; PMCID: PMC2861645.
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Proteome Sci. 2010 Apr 13;8:22. doi: 10.1186/1477-5956-8-22.

Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry.

Proteome science

Maxim Isabelle, Xavier Moreel, Jean-Philippe Gagné, Michèle Rouleau, Chantal Ethier, Pierre Gagné, Michael J Hendzel, Guy G Poirier

Affiliations

  1. Axe cancer, CHUQ Research Center, Faculty of Medicine, Laval University, 2705 Boulevard Laurier, Québec, Canada, G1V 4G2. [email protected].

PMID: 20388209 PMCID: PMC2861645 DOI: 10.1186/1477-5956-8-22

Abstract

BACKGROUND: Poly(ADP-ribose) polymerases (PARPs) catalyze the formation of poly(ADP-ribose) (pADPr), a post-translational modification involved in several important biological processes, namely surveillance of genome integrity, cell cycle progression, initiation of the DNA damage response, apoptosis, and regulation of transcription. Poly(ADP-ribose) glycohydrolase (PARG), on the other hand, catabolizes pADPr and thereby accounts for the transient nature of poly(ADP-ribosyl)ation. Our investigation of the interactomes of PARP-1, PARP-2, and PARG by affinity-purification mass spectrometry (AP-MS) aimed, on the one hand, to confirm current knowledge on these interactomes and, on the other hand, to discover new protein partners which could offer insights into PARPs and PARG functions.

RESULTS: PARP-1, PARP-2, and PARG were immunoprecipitated from human cells, and pulled-down proteins were separated by gel electrophoresis prior to in-gel trypsin digestion. Peptides were identified by tandem mass spectrometry. Our AP-MS experiments resulted in the identifications of 179 interactions, 139 of which are novel interactions. Gene Ontology analysis of the identified protein interactors points to five biological processes in which PARP-1, PARP-2 and PARG may be involved: RNA metabolism for PARP-1, PARP-2 and PARG; DNA repair and apoptosis for PARP-1 and PARP-2; and glycolysis and cell cycle for PARP-1.

CONCLUSIONS: This study reveals several novel protein partners for PARP-1, PARP-2 and PARG. It provides a global view of the interactomes of these proteins as well as a roadmap to establish the systems biology of poly(ADP-ribose) metabolism.

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