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Preferential Perinuclear Localization of Poly(ADP-ribose) Glycohydrolase
Authors:Eric Winstall   El Bachir Affar   Rashmi Shah   Sylvie Bourassa   Ivana A. Scovassi  Guy G. Poirier  
Affiliation:Faculty of Medicine, Laval University Medical Research Center, Québec, G1V 4G2, Canada.
Abstract:The transient nature of poly(ADP-ribosyl)ation, a posttranslational modification of nuclear proteins, is achieved by the enzyme poly(ADP-ribose) glycohydrolase (PARG) which hydrolyzes the poly(ADP-ribose) polymer into free ADP-ribose residues. To investigate the molecular size and localization of PARG, we developed a specific polyclonal antibody directed against the bovine PARG carboxy-terminal region. We found that PARG purified from bovine thymus was recognized as a 59-kDa protein, while Western blot analysis of total cell extracts revealed the presence of a unique 110-kDa protein. This 110-kDa PARG was mostly found in postnuclear extracts, whereas it was barely detectable in the nuclear fractions of COS7 cells. Further analysis by immunofluorescence revealed a cytoplasmic perinuclear distribution of PARG in COS7 cells overexpressing the bovine PARG cDNA. These results provide direct evidence that PARG is primarily a cytoplasmic enzyme and suggest that a very low amount of intranuclear PARG is required for poly(ADP-ribose) turnover.
Keywords:poly(ADP-ribose) glycohydrolase   posttranslational modification   DNA damage   immunocytochemistry   anti-peptide antibody
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