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Titolo:
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
Autore:
DAmours, D; Desnoyers, S; DSilva, I; Poirier, GG;
Indirizzi:
Wellcome, CRC, Inst Canc & Dev Biol, Cambridge CB2 1QR, England Wellcome Cambridge England CB2 1QR Dev Biol, Cambridge CB2 1QR, England Cold Spring Harbor Lab, Cold Spring Harbor, NY 11724 USA Cold Spring Harbor Lab Cold Spring Harbor NY USA 11724 rbor, NY 11724 USA Univ Laval, CHUQ, Med Res Ctr, Hlth & Environm Unit, Quebec City, PQ G1V 4G2, Canada Univ Laval Quebec City PQ Canada G1V 4G2 Quebec City, PQ G1V 4G2, Canada Univ Laval, Fac Med, Dept Med Biol, Quebec City, PQ G1K 7P4, Canada Univ Laval Quebec City PQ Canada G1K 7P4 Quebec City, PQ G1K 7P4, Canada
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 342, anno: 1999,
parte:, 2
pagine: 249 - 268
SICI:
0264-6021(19990901)342:<249:PRITRO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLY(ADENOSINE DIPHOSPHATE RIBOSE); NICOTINAMIDE ADENINE-DINUCLEOTIDE; DNA-STRAND-BREAKS; RNA-POLYMERASE-II; POLY-ADP-RIBOSYLATION; SISTER-CHROMATID EXCHANGES; INTRACHROMOSOMAL HOMOLOGOUS RECOMBINATION; CELLULAR-ENERGY DEPLETION; MOBILITY GROUP PROTEIN-1; MOLECULAR NICK-SENSOR;
Keywords:
chromatin structure; DNA repair; genome integrity; poly(ADP-ribose) glycohydrolase; poly(ADP-ribose) polymerase;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
346
Recensione:
Indirizzi per estratti:
Indirizzo: Poirier, GG CHU Laval, CHUQ, Ctr Rech, Unite Rech Sante & Environm, 2705 Blvd Laurier,Quebec City, PQ G1V 4G2, Canada CHU Laval 2705 Blvd Laurier Quebec City PQ Canada G1V 4G2 nada
Citazione:
D. D'Amours et al., "Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions", BIOCHEM J, 342, 1999, pp. 249-268

Abstract

Poly(ADP-ribosyl)ation is a post-translational modification of proteins. During this process, molecules of ADP-ribose are added successively on to acceptor proteins to form branched polymers. This modification is transient but very extensive in vivo, as polymer chains can reach more than 200 units on protein accepters. The existence of the poly(ADP-ribose) polymer was first reported nearly 40 years ago. Since then, the importance of poly(ADP-ribose) synthesis has been established in many cellular processes. However, a clear and unified picture of the physiological role of poly(ADP-ribosyl)ation still remains to be established. The total dependence of poly(ADP-ribose) synthesis on DNA. strand breaks strongly suggests that this posttranslational modification is involved in the metabolism of nucleic acids. This viewis also supported by the identification of direct protein-protein interactions involving poly(ADP-ribose) polymerase (113 kDa PARP), an enzyme catalysing the formation of poly(ADP-ribose), and key effecters of DNA repair, replication and transcription reactions. The presence of PARP in these multiprotein complexes, in addition to the actual poly(ADP-ribosyl)ation of some components of these complexes, clearly supports an important role for poly(ADP-ribosyl)ation reactions in DNA transactions. Accordingly, inhibition ofpoly(ADP-ribose) synthesis by any of several approaches and the analysis of PARP-deficient cells has revealed that the absence of poly(ADP-ribosyl)ation strongly affects DNA metabolism, most notably DNA repair. The recent identification of new poly(ADP-ribosyl)ating enzymes with distinct (non-standard) structures in eukaryotes and archaea has revealed a novel level of complexity in the regulation of poly(ADP-ribose) metabolism.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 11:43:39