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Titolo:
Mre11 and Rad50 from Pyrococcus furiosus: Cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine
Autore:
Hopfner, KP; Karcher, A; Shin, D; Fairley, C; Tainer, JA; Carney, JP;
Indirizzi:
Univ Maryland, Sch Med, Radiat Oncol Res Lab, Baltimore, MD 21201 USA UnivMaryland Baltimore MD USA 21201 col Res Lab, Baltimore, MD 21201 USA Univ Maryland, Sch Med, Marlene & Stewart Greenebaum Canc Ctr, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 um Canc Ctr, Baltimore, MD 21201 USA Univ Calif Berkeley, Lawrence Berkeley Lab, Div Life Sci, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 ife Sci, Berkeley, CA 94720 USA Scripps Clin & Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA Scripps Clin & Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA
Titolo Testata:
JOURNAL OF BACTERIOLOGY
fascicolo: 21, volume: 182, anno: 2000,
pagine: 6036 - 6041
SICI:
0021-9193(200011)182:21<6036:MARFPF>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
STRAND BREAK REPAIR; ESCHERICHIA-COLI K-12; SACCHAROMYCES-CEREVISIAE; GENETIC-RECOMBINATION; PROTEIN COMPLEX; DNA PALINDROMES; MAINTENANCE; BINDING; YEAST; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Carney, JP Univ Maryland, Sch Med, Radiat Oncol Res Lab, Bressler Res Bldg,6-015,655 W Baltimore St, Baltimore, MD 21201 USA Univ Maryland Bressler Res Bldg,6-015,655 W Baltimore St Baltimore MD USA 21201
Citazione:
K.P. Hopfner et al., "Mre11 and Rad50 from Pyrococcus furiosus: Cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine", J BACT, 182(21), 2000, pp. 6036-6041

Abstract

The processing of DNA double-strand breaks is a critical event in nucleic acid metabolism. This is evidenced by the severity of phenotypes associatedwith deficiencies in this process in multiple organisms. The core component involved in double-strand break repair in eukaryotic cells is the Mre11-Rad50 protein complex, which includes a third protein, p95, in humans and Xrs2 in yeasts. Homologues of Mre11 and Rad50 have been identified in all kingdoms of life, while the Nbs1 protein family is found only in eukaryotes. In eukaryotes the Mre11-Rad50 complex has nuclease activity that is modulated by the addition of ATP. We have isolated the Mre11 and Rad50 homologues from the thermophilic archaeon Pyrococcus furiosus and demonstrate that the two proteins exist in a large, heat-stable complex that possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. These findings verify the identification of the P. furiosus Rad50 and Mre11 homologues and demonstrate that functional homologues with similar biochemical properties exist in all kingdoms of life.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 20:13:05