ANTONY, Edwin, Eric J. TOMKO, Qi XIAO, Lumír KREJČÍ, Timothy M. LOHMAN and Tom ELLENBERGER. Srs2 Disassembles Rad51 Filaments by a Protein-Protein Interaction Triggering ATP Turnover and Dissociation of Rad51 from DNA. Molecular Cell. 2009, vol. 35, No 1, p. 105-115, 10 pp. ISSN 1097-2765.
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Basic information
Original name Srs2 Disassembles Rad51 Filaments by a Protein-Protein Interaction Triggering ATP Turnover and Dissociation of Rad51 from DNA
Name in Czech Srs2 protein rozpouští Rad51 vlákna díky protein-protein interakčně spuštěné hydrolýze ATP
Authors ANTONY, Edwin (840 United States of America), Eric J. TOMKO (840 United States of America), Qi XIAO (840 United States of America), Lumír KREJČÍ (203 Czech Republic, guarantor), Timothy M. LOHMAN (840 United States of America) and Tom ELLENBERGER (840 United States of America).
Edition Molecular Cell, 2009, 1097-2765.
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: 14.608
RIV identification code RIV/00216224:14310/09:00029284
Organization unit Faculty of Science
UT WoS 000268003300010
Keywords in English DNA repair; DNA damage; replication; genomic instability
Tags DNA damage, DNA repair, genomic instability, replication
Tags International impact, Reviewed
Changed by Changed by: doc. Mgr. Lumír Krejčí, Ph.D., učo 18098. Changed: 17/7/2009 12:25.
Abstract
Rad51 is a DNA recombinase functioning in the repair of DNA double-strand breaks and the generation of genetic diversity by homologous recombination (HR). In the presence of ATP, Rad51 self-assembles into an extended polymer on single-stranded DNA to catalyze strand exchange. Inappropriate HR causes genomic instability and it is normally prevented by remodeling enzymes that antagonize the activities of Rad51 nucleoprotein filaments. In yeast, the Srs2 helicase/translocase suppresses HR by clearing Rad51 polymers from single-stranded DNA. We have examined the mechanism of disassembly of Rad51 nucleoprotein filaments by Srs2 and find that a physical interaction between Rad51 and the C-terminal region of Srs2 triggers ATP hydrolysis within the Rad51 filament, causing Rad51 to dissociate from DNA. This allosteric mechanism explains the biological specialization of Srs2 as a DNA motor protein that antagonizes HR.
Abstract (in Czech)
Charakterizace působení Srs2 proteinu na Rad51 nukleoproteinové vlákno
Links
GA301/09/1917, research and development projectName: Štěpení replikačních-rekombinačních DNA meziproduktů a jejich úloha při nestabilitě genomu
Investor: Czech Science Foundation
GD203/09/H046, research and development projectName: Biochemie na rozcestí mezi in silico a in vitro
Investor: Czech Science Foundation
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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