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Updated: Aug 16, 2026

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
Published on: January 16, 2017
Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles
Jean-Philippe Gagné1, Marie-Eve Bonicalzi, Pierre Gagné
1Health and Environment Unit, Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, 2705 Boulevard Laurier, Ste-Foy, Québec, Canada, G1V 4G2.
Abstract:
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.
Insights
Poly(ADP-ribose) glycohydrolase (PARG) was identified in Fragile-X mental retardation protein (FMRP)-associated complexes. This suggests a role for PARG in translational regulation beyond DNA repair.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Poly(ADP-ribosyl)ation is a post-translational modification regulating protein function, primarily studied in DNA damage response.
- Poly(ADP-ribose) glycohydrolase (PARG) is the sole enzyme responsible for hydrolyzing poly(ADP-ribose) chains.
- Emerging evidence indicates poly(ADP-ribosyl)ation has broader cellular roles beyond DNA transactions.
Purpose of the Study:
- To identify proteins interacting with PARG.
- To elucidate novel cellular functions of PARG.
- To investigate the role of PARG in translational regulation.
Main Methods:
- Proteomic identification of PARG-interacting proteins using mass spectrometry.
- Co-immunoprecipitation and pull-down assays to isolate PARG complexes.
- Sedimentation analysis and microscopy to confirm PARG localization.
Main Results:
- PARG was identified as a component of Fragile-X mental retardation protein (FMRP)-associated messenger ribonucleoprotein complexes.
- PARG's localization within these complexes, part of the translation machinery, was confirmed.
- A functional connection between poly(ADP-ribosyl)ation and FMRP-associated complexes was suggested.
Conclusions:
- PARG is involved in the regulation of translation through its association with FMRP-RNP complexes.
- This finding expands the known functions of PARG beyond DNA repair pathways.
- PARG's role in translational regulation warrants further investigation.
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