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@article{945695,
author = {Šebesta, Marek and Burkovics, Peter and Haracska, Lajos and Krejčí, Lumír},
article_number = {6},
doi = {http://dx.doi.org/10.1016/j.dnarep.2011.03.003},
keywords = {DNA repair; Recombination; DNA synthesis; Replication; Mph1 Srs2},
language = {eng},
issn = {1568-7864},
journal = {DNA Repair},
title = {Reconstitution of DNA repair synthesis in vitro and the role of polymerase and helicase activities},
volume = {10},
year = {2011}
}
TY - JOUR
ID - 945695
AU - Šebesta, Marek - Burkovics, Peter - Haracska, Lajos - Krejčí, Lumír
PY - 2011
TI - Reconstitution of DNA repair synthesis in vitro and the role of polymerase and helicase activities
JF - DNA Repair
VL - 10
IS - 6
SP - 567-576
EP - 567-576
SN - 15687864
KW - DNA repair
KW - Recombination
KW - DNA synthesis
KW - Replication
KW - Mph1 Srs2
N2 - The error-free repair of double-strand DNA breaks by homologous recombination (HR) ensures genomic stability using undamaged homologous sequence to copy genetic information. While some of the aspects of the initial steps of HR are understood, the molecular mechanisms underlying events downstream of the D-loop formation remain unclear. Therefore, we have reconstituted D-loop-based in vitro recombinationassociated DNA repair synthesis assay and tested the efficacy of polymerases Pol and Pol to extend invaded primer, and the ability of three helicases (Mph1, Srs2 and Sgs1) to displace this extended primer. Both Pol and Pol extended up to 50% of the D-loop substrate, but differed in product length and dependency on proliferating cell nuclear antigen (PCNA). Mph1, but not Srs2 or Sgs1, displaced the extended primer very efficiently, supporting putative role ofMph1in promoting the synthesis-dependent strand-annealing pathway. The experimental system described here can be employed to increase our understanding of HR events following D-loop formation, as well as the regulatory mechanisms involved.
ER -
ŠEBESTA, Marek, Peter BURKOVICS, Lajos HARACSKA a Lumír KREJČÍ. Reconstitution of DNA repair synthesis in vitro and the role of polymerase and helicase activities. \textit{DNA Repair}. roč.~10, č.~6, s.~567-576. ISSN~1568-7864. doi:10.1016/j.dnarep.2011.03.003. 2011.
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