PARG

PARG
Poly (ADP-ribose) glycohydrolase
Identifiers
Symbols PARG; FLJ54459; FLJ60257; FLJ60456; PARG99
External IDs OMIM: 603501 HomoloGene: 50532 GeneCards: PARG Gene
EC number 3.2.1.143
Orthologs
Species Human Mouse
Entrez 8505 26430
Ensembl ENSG00000227345 ENSMUSG00000021911
UniProt Q86W56 O88622
RefSeq (mRNA) NM_003631.2 NM_011960.2
RefSeq (protein) NP_003622.2 NP_036090.2
Location (UCSC) Chr 10:
51.03 – 51.13 Mb		 Chr 14:
33.02 – 33.11 Mb
PubMed search [1] [2]
This box: view · enzyme that in humans is encoded by the PARG gene.[1][2][3]

Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins. The protein is found in many tissues and may be subject to proteolysis generating smaller, active products.[1]

References

  1. ^ a b "Entrez Gene: Poly (ADP-ribose) glycohydrolase". http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=8505. Retrieved 2011-11-08T12:08:44.097-08:00. 
  2. ^ Lin W, Amé JC, Aboul-Ela N, Jacobson EL, Jacobson MK (May 1997). "Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase". J. Biol. Chem. 272 (18): 11895–901. PMID 9115250. 
  3. ^ Amé JC, Apiou F, Jacobson EL, Jacobson MK (1999). "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization". Cytogenet. Cell Genet. 85 (3-4): 269–70. PMID 10449915. 

Further reading

  • Affar, E. B.; Germain, M.; Winstall, E.; Vodenicharov, M.; Shah, R. G.; Salvesen, G. S.; Poirier, G. G. (2000). "Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis". Journal of Biological Chemistry 276 (4): 2935–2942. doi:10.1074/jbc.M007269200. PMID 11053413.  edit
  • Ohashi, S.; Kanai, M.; Hanai, S.; Uchiumi, F.; Maruta, H.; Tanuma, S.; Miwa, M. (2003). "Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells". Biochemical and biophysical research communications 307 (4): 915–921. PMID 12878198.  edit
  • Meyer, R. G.; Meyer-Ficca, M. L.; Jacobson, E. L.; Jacobson, M. K. (2003). "Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)". Gene 314: 181–190. PMID 14527731.  edit
  • Golovanov, A. P.; Barillà, D.; Golovanova, M.; Hayes, F.; Lian, L. Y. (2003). "ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure". Molecular microbiology 50 (4): 1141–1153. PMID 14622405.  edit
  • Keil, C.; Petermann, E.; Oei, S. L. (2004). "Tannins elevate the level of poly(ADP–ribose) in HeLa cell extracts". Archives of Biochemistry and Biophysics 425 (1): 115–121. doi:10.1016/j.abb.2004.02.024. PMID 15081900.  edit
  • Meyer-Ficca, M. L.; Meyer, R. G.; Coyle, D. L.; Jacobson, E. L.; Jacobson, M. K. (2004). "Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments". Experimental Cell Research 297 (2): 521–532. doi:10.1016/j.yexcr.2004.03.050. PMID 15212953.  edit
  • Putt, K. S.; Hergenrother, P. J. (2004). "A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): Application to inhibitor identification and evaluation". Analytical Biochemistry 333 (2): 256–264. doi:10.1016/j.ab.2004.04.032. PMID 15450800.  edit
  • Bonicalzi, M. -E.; Haince, J. -F.; Droit, A.; Poirier, G. G. (2005). "Poly-ADP-ribosylation in health and disease". CMLS Cellular and Molecular Life Sciences 62 (7–8): 739–750. doi:10.1007/s00018-004-4505-1. PMID 15868399.  edit
  • Bonicalzi, M. È.; Gagné, J. P.; Gagné, P.; Ouellet, M. È.; Hendzel, M. J.; Poirier, G. G. (2005). "Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles". Biochemical Journal 392 (3): 499–509. doi:10.1042/BJ20050792. PMC 1316289. PMID 16117724. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1316289.  edit

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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