| Literature DB >> 27668604 |
S N Khodyreva1, O I Lavrik1,2.
Abstract
Poly(ADP-ribosyl)ation (PARylation) of proteins is one of the immediate cell responses to DNA damage and is catalyzed by poly(ADP-ribose) polymerases (PARPs). When bound to damaged DNA, some members of the PARP family are activated and use NAD^(+) as a source of ADP to catalyze synthesis of poly(ADP-ribose) (PAR) covalently attached to a target protein. PAR synthesis is considered as a mechanism that provides a local signal of DNA damage and modulates protein functions in response to genotoxic agents. PARP1 is the best-studied protein of the PARP family and is widely known аs a regulator of repair of damaged bases and single-strand nicks. Data are accumulating that PARP1 is additionally involved in double-strand break repair and nucleotide excision repair. The review summarizes the literature data on the role that PARP1 and PARylation play in DNA repair and particularly in base excision repair; original data obtained in our lab are considered in more detail.Entities:
Keywords: DNA repair; poly(ADP-ribose) polymerase 1; poly(ADP-ribosyl)ation; protein-nucleic acid interaction
Year: 2016 PMID: 27668604 DOI: 10.7868/S0026898416040030
Source DB: PubMed Journal: Mol Biol (Mosk) ISSN: 0026-8984