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Biochim Biophys Acta. 2006 Feb;1763(2):226-37. Epub 2005 Dec 27.

Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage.

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1
Health and Environment Unit, Laval University Hospital Research Center, CHUQ, Faculty of Medicine, Laval University, Room RC-9700, 2705 Laurier blvd., Ste-Foy, Qu├ębec, Canada G1V 4G2.

Abstract

Poly(ADP-ribosyl)ation is a very early cellular response to DNA damage. Poly(ADP-ribose) (PAR) accumulation is transient since PAR is rapidly hydrolyzed by poly(ADP-ribose) glycohydrolase (PARG). PARG may play a prominent role in DNA damage response and repair by removing PAR from modified proteins including PARP-1. Using living cells, we provide evidence that in response to DNA damage induced by gamma-irradiation the cytoplasmic 103 kDa PARG isoform translocates into the nucleus. We further observed that the nuclear GFP-hPARG110 enzyme relocalizes to the cytoplasm in response to DNA damage. Using different GFP-PARG fusion proteins specific for the nuclear and cytoplasmic forms, we demonstrate their dynamic distribution between cytoplasm and nucleoplasm and a high mobility of major PARG isoforms by fluorescence recovery after photobleaching (FRAP). The dynamic relocation of all PARG isoforms presented in this report reveals a novel biological mechanism by which PARG could be involved in DNA damage response.

PMID:
16460818
DOI:
10.1016/j.bbamcr.2005.11.015
[Indexed for MEDLINE]
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