Unwinding of synthetic replication and recombination substrates by Srs2

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.

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

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Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

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

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Abstract

V originále

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).

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Links

GAP207/12/2323, research and development project	Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I Investor: Czech Science Foundation
GA301/09/1917, research and development project	Name: Štěpení replikačních-rekombinačních DNA meziproduktů a jejich úloha při nestabilitě genomu Investor: Czech Science Foundation
GD203/09/H046, research and development project	Name: Biochemie na rozcestí mezi in silico a in vitro Investor: Czech Science Foundation
ME10048, research and development project	Name: 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)