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Titolo:
Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase
Autore:
Hopfner, KP; Karcher, A; Craig, L; Woo, TT; Carney, JP; Tainer, JA;
Indirizzi:
Scripps Clin & Res Fdn, Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Clin & Res Fdn La Jolla CA USA 92037 Biol, La Jolla, CA 92037 USA Scripps Clin & Res Fdn, Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA Scripps Clin & Res Fdn La Jolla CA USA 92037 Biol, La Jolla, CA 92037 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 Univ Maryland, Sch Med, Marlene & Stewart Greenebaum Canc Ctr, Dept RadiatOncol,Radiat Oncol Res Lab, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 col Res Lab, Baltimore, MD 21201 USA Univ Maryland, Sch Med, Mol & Cell Biol Grad Program, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 rad Program, Baltimore, MD 21201 USA
Titolo Testata:
CELL
fascicolo: 4, volume: 105, anno: 2001,
pagine: 473 - 485
SICI:
0092-8674(20010518)105:4<473:SBAIAO>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; IONIZING-RADIATION; MISMATCH REPAIR; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; PROTEIN COMPLEX; CHROMOSOMES SMC; MAMMALIAN-CELLS; RECOMBINATION; RAD50;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Tainer, JA Scripps Clin & Res Fdn, Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Clin & Res Fdn La Jolla CA USA 92037 lla, CA 92037 USA
Citazione:
K.P. Hopfner et al., "Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase", CELL, 105(4), 2001, pp. 473-485

Abstract

To clarify functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair, we report Pyrococcus furiosus Mre11 crystal structures, revealing a protein phosphatase-like, dimanganese binding domain capped by a unique domain controlling active site access. These structures unify Mre11's multiple nuclease activities in a single endo/exonuclease mechanism and reveal eukaryotic macromolecular interaction sites by mapping human and yeast Mre11 mutations. Furthermore, the structure of the P. furiosus Rad50 ABC-ATPase with its adjacent coiled-coil defines a compact Mre11/Rad50-ATPase complex and suggests that Rad50-ATP-driven conformational switching directly controls the Mre11 exonuclease. Electron microscopy, small angle X-ray scattering, and ultracentrifugation data of human and P. furiosus MR reveal a dual functional complex consisting of a (Mre11)(2)/(Rad50)(2) heterotetramericDNA processing head and a double coiled-coil linker.

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Documento generato il 22/09/20 alle ore 18:46:16