Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles

被引:17
作者
Gagné, JP
Bonicalzi, ME
Gagné, P
Ouellet, ME
Hendzel, MJ
Poirier, GG
机构
[1] Univ Laval, Fac Med, CHUQ,Med Res Ctr, Hlth & Environm Unit, Ste Foy, PQ G1V 4G2, Canada
[2] Univ Alberta, Dept Oncol, Edmonton, AB T6G 1Z2, Canada
[3] Univ Laval, Med Res Ctr, Eastern Quebec Proteom Ctr, Ste Foy, PQ G1V 4G2, Canada
关键词
fragile-X; messenger ribonucleoparticle (mRNP); poly (ADP-ribose) glycohydrolase (PARG); proteomics; translational regulation;
D O I
10.1042/BJ20050792
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:499 / 509
页数:11
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