Unwinding of synthetic replication and recombination substrates by Srs2

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F12%3A00057534" target="_blank" >RIV/00216224:14310/12:00057534 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00159816:_____/12:#0000964

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.dnarep.2012.05.007" target="_blank" >http://dx.doi.org/10.1016/j.dnarep.2012.05.007</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.dnarep.2012.05.007" target="_blank" >10.1016/j.dnarep.2012.05.007</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Unwinding of synthetic replication and recombination substrates by Srs2

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Unwinding of synthetic replication and recombination substrates by Srs2

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

DNA Repair

ISSN

1568-7864

e-ISSN

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Svazek periodika

11

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

789-798

Kód UT WoS článku

000310761100002

EID výsledku v databázi Scopus

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