KREJČÍ, Lumír, Stephen VAN KOMEN, Ying LI, Jane VILLEMAIN, Sredhar REDDY, Hannah KLEIN, Tom ELLENBERGER and Patrick SUNG. DNA helicase Srs2 disrupts the Rad51 presynaptic filament. Nature. Lodon, UK: Nature Publishing Group, 2003, vol. 423, No 6937, p. 305-9, 4 pp. ISSN 0028-0836.
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Basic information
Original name DNA helicase Srs2 disrupts the Rad51 presynaptic filament.
Name in Czech DNA helicase Srs2 disrupts the Rad51 presynaptic filament.
Authors KREJČÍ, Lumír (203 Czech Republic, guarantor), Stephen VAN KOMEN (840 United States of America), Ying LI (840 United States of America), Jane VILLEMAIN (840 United States of America), Sredhar REDDY (356 India), Hannah KLEIN (840 United States of America), Tom ELLENBERGER (840 United States of America) and Patrick SUNG (840 United States of America).
Edition Nature, Lodon, UK, Nature Publishing Group, 2003, 0028-0836.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 30.979
Organization unit Faculty of Science
Keywords in English recombination; repair; Srs2;Rad51
Tags Rad51, recombination, repair, Srs2
Tags International impact, Reviewed
Changed by Changed by: doc. Mgr. Lumír Krejčí, Ph.D., učo 18098. Changed: 15/5/2009 22:59.
Abstract
Mutations in the Saccharomyces cerevisiae gene SRS2 result in the yeast's sensitivity to genotoxic agents, failure to recover or adapt from DNA damage checkpoint-mediated cell cycle arrest, slow growth, chromosome loss, and hyper-recombination. Furthermore, double mutant strains, with mutations in DNA helicase genes SRS2 and SGS1, show low viability that can be overcome by inactivating recombination, implying that untimely recombination is the cause of growth impairment. Here we clarify the role of SRS2 in recombination modulation by purifying its encoded product and examining its interactions with the Rad51 recombinase. Srs2 has a robust ATPase activity that is dependent on single-stranded DNA (ssDNA) and binds Rad51, but the addition of a catalytic quantity of Srs2 to Rad51-mediated recombination reactions causes severe inhibition of these reactions. We show that Srs2 acts by dislodging Rad51 from ssDNA. Thus, the attenuation of recombination efficiency by Srs2 stems primarily from its ability to dismantle the Rad51 presynaptic filament efficiently. Our findings have implications for the basis of Bloom's and Werner's syndromes, which are caused by mutations in DNA helicases and are characterized by increased frequencies of recombination and a predisposition to cancers and accelerated ageing.
Abstract (in Czech)
Srs2 a jeho anti-rekombinační aktivita
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