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Literature summary for 3.2.1.143 extracted from

  • Gao, H.; Coyle, D.L.; Meyer-Ficca, M.L.; Meyer, R.G.; Jacobson, E.L.; Wang, Z.Q.; Jacobson, M.K.
    Altered poly(ADP-ribose) metabolism impairs cellular responses to genotoxic stress in a hypomorphic mutant of poly(ADP-ribose) glycohydrolase (2007), Exp. Cell Res., 313, 984-996.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information hypomorphic mouse model in which exons 2 and 3 of PARG gene have been deleted. Mutants exhibits nuclear localization of the enzyme which contains a catalytic domain but lacks the N-terminal region. Following DNA damage induced by N-methyl-N'-nitro-N-nitrosoguanidine, activity of both poly(ADP-ribose) glycohydrolase and poly(ADP-ribose) polymerase in mutant cell increases. Increase in poly(ADP-ribose) glycohydrolase activity leads to decrease in poly(ADP-ribose) polymerase-1 automodification resulting in increased activity. Mutant cells also show reduced formation of XCRR1 foci, delayed H2AX phosphorylation, decreased DNA break intermediates during repair, and increased cell death Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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hypomorphic mouse model in which exons 2 and 3 of PARG gene have been deleted
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