PARG [poly(ADP-ribose) glycohydrolase] is the only known enzyme that catalyses the hydrolysis of poly(ADP-ribose), a branched polymer that is synthesized by the poly(ADP-ribose) polymerase family of enzymes. Poly(ADP-ribosyl)ation is a transient post-translational modification that alters the functions of the acceptor proteins. It has mostly been studied in the context of DNA-damage signalling or DNA transaction events, such as replication and transcription reactions. Growing evidence now suggests that poly(ADP-ribosyl)ation could have a much broader impact on cellular functions. To elucidate the roles that could be played by PARG, we performed a proteomic identification of PARG-interacting proteins by mass spectrometric analysis of PARG pulled-down proteins. In the present paper, we report that PARG is resident in FMRP (Fragile-X mental retardation protein)-associated messenger ribonucleoparticles complexes. The localization of PARG in these complexes, which are components of the translation machinery, was confirmed by sedimentation and microscopy analysis. A functional link between poly(ADP-ribosyl)ation modulation and FMRP-associated ribonucleoparticle complexes are discussed in a context of translational regulation.
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Research Article|
December 06 2005
Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles
Jean-Philippe Gagné;
Jean-Philippe Gagné
*Health and Environment Unit, Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, 2705 Boulevard Laurier, Ste-Foy, Québec, Canada, G1V 4G2
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Marie-Ève Bonicalzi;
Marie-Ève Bonicalzi
*Health and Environment Unit, Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, 2705 Boulevard Laurier, Ste-Foy, Québec, Canada, G1V 4G2
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Pierre Gagné;
Pierre Gagné
*Health and Environment Unit, Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, 2705 Boulevard Laurier, Ste-Foy, Québec, Canada, G1V 4G2
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Marie-Ève Ouellet;
Marie-Ève Ouellet
*Health and Environment Unit, Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, 2705 Boulevard Laurier, Ste-Foy, Québec, Canada, G1V 4G2
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Michael J. Hendzel;
Michael J. Hendzel
†Department of Oncology, University of Alberta, Edmonton, Alberta, Canada, T6G 1Z2
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Guy G. Poirier
Guy G. Poirier
1
*Health and Environment Unit, Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, 2705 Boulevard Laurier, Ste-Foy, Québec, Canada, G1V 4G2
‡Eastern Quebec Proteomic Center, Laval University Medical Research Center, 2705 Boulevard Laurier, Ste-Foy, Québec, Canada, G1V 4G2
1To whom correspondence should be addressed (email guy.poirier@crchul.ulaval.ca).
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Publisher: Portland Press Ltd
Received:
May 12 2005
Revision Received:
July 28 2005
Accepted:
August 23 2005
Accepted Manuscript online:
August 23 2005
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2005
Biochem J (2005) 392 (3): 499–509.
Article history
Received:
May 12 2005
Revision Received:
July 28 2005
Accepted:
August 23 2005
Accepted Manuscript online:
August 23 2005
Citation
Jean-Philippe Gagné, Marie-Ève Bonicalzi, Pierre Gagné, Marie-Ève Ouellet, Michael J. Hendzel, Guy G. Poirier; Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles. Biochem J 15 December 2005; 392 (3): 499–509. doi: https://doi.org/10.1042/BJ20050792
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