MARINI PALOMEQUE, María Victoria and Lumír KREJČÍ. Unwinding of synthetic replication and recombination substrates by Srs2. DNA Repair. ELSEVIER, 2012, vol. 11, No 10, p. 789-798. ISSN 1568-7864. Available from: https://dx.doi.org/10.1016/j.dnarep.2012.05.007.
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Basic information
Original name Unwinding of synthetic replication and recombination substrates by Srs2
Authors MARINI PALOMEQUE, María Victoria (858 Uruguay, belonging to the institution) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution).
Edition DNA Repair, ELSEVIER, 2012, 1568-7864.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 4.274
RIV identification code RIV/00216224:14310/12:00057534
Organization unit Faculty of Science
Doi http://dx.doi.org/10.1016/j.dnarep.2012.05.007
UT WoS 000310761100002
Keywords in English DNA repair; Recombination; Srs2; Replication; Helicase
Tags AKR, rivok
Tags International impact, Reviewed
Changed by Changed by: Ing. Andrea Mikešková, učo 137293. Changed: 22/4/2013 14:51.
Abstract
The budding yeast Srs2 protein possesses 3 to 5 DNA helicase activity and channels untimely recombination to post-replication repair by removing Rad51 from ssDNA. However, it also promotes recombination via a synthesis-dependent strand-annealing pathway (SDSA). Furthermore, at the replication fork, Srs2 is required for fork progression and prevents the instability of trinucleotide repeats. To better understand the multiple roles of the Srs2 helicase during these processes, we analysed the ability of Srs2 to bind and unwind various DNA substrates that mimic structures present during DNA replication and recombination. While leading or lagging strands were efficiently unwound, the presence of ssDNA binding protein RPA presented an obstacle for Srs2 translocation. We also tested the preferred directionality of unwinding of various substrates and studied the effect of Rad51 and Mre11 proteins on Srs2 helicase activity. These biochemical results help us understand the possible role of Srs2 in the processing of stalled or blocked replication forks as a part of post-replication repair as well as homologous recombination (HR).
Links
GAP207/12/2323, research and development projectName: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
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
ME10048, research and development projectName: Vliv post-translačních modifikací na DNA opravu a rekombinaci.
Investor: Ministry of Education, Youth and Sports of the CR, Research and Development Programme KONTAKT (ME)
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