Unwinding of synthetic replication and recombination substrates by Srs2

Logo poskytovatele
Logo poskytovatele

Varování

Publikace nespadá pod Fakultu sportovních studií, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
Autoři

MARINI PALOMEQUE María Victoria KREJČÍ Lumír

Rok publikování 2012
Druh Článek v odborném periodiku
Časopis / Zdroj DNA Repair
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www http://www.sciencedirect.com/science/article/pii/S1568786412001826#
Doi http://dx.doi.org/10.1016/j.dnarep.2012.05.007
Obor Biochemie
Klíčová slova DNA repair; Recombination; Srs2; Replication; Helicase
Popis 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).
Související projekty:

Používáte starou verzi internetového prohlížeče. Doporučujeme aktualizovat Váš prohlížeč na nejnovější verzi.

Další info