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Biochem Cell Biol. 2005 Jun;83(3):263-9.

Poly(ADP-ribosylation) and genomic stability.

Author information

1
Freie Universität Berlin, Institut für Biochemie, Germany. lity@chemie.fu-berlin.de

Abstract

Poly(ADP-ribose) polymerases (PARPs) catalyze the synthesis of ADP-ribose polymers and attach them to specific target proteins. To date, 6 members of this protein family in humans have been characterized. The best-known PARP, PARP-1, is located within the nucleus and has a major function in DNA repair but also in the execution of cell death pathways. Other PARP enzymes appear to carry out highly specific functions. Most prominently, the tankyrases modify telomere-binding proteins and thereby regulate telomere maintenance. Since only a single enzyme, poly(ADP-ribose) glycohydrolase (PARG), has been identified, which degrades poly(ADP-ribose), it is expected that this protein has important roles in PARP-mediated regulatory processes. This review summarizes recent observations indicating that poly(ADP-ribosylation) represents a major mechanism to regulate genomic stability both when DNA is damaged by exogenous agents and during cell division.

PMID:
15959554
DOI:
10.1139/o05-039
[Indexed for MEDLINE]

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