Journal ArticleDOI
Interplay of replication checkpoints and repair proteins at stalled replication forks.
Dana Branzei,Marco Foiani +1 more
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TLDR
This review focuses mainly on the results obtained in budding yeast on the multiple roles of checkpoints in maintaining fork integrity and on the enzymatic activities that cooperate with the checkpoint pathway to promote fork resumption and repair of DNA lesions thereby contributing to genome integrity.About:
This article is published in DNA Repair.The article was published on 2007-07-01. It has received 144 citations till now. The article focuses on the topics: Control of chromosome duplication & DNA re-replication.read more
Citations
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Journal ArticleDOI
An oncogene-induced DNA damage model for cancer development.
TL;DR: Oncogene-induced DNA damage may explain two key features of cancer: genomic instability and the high frequency of p53 mutations.
Journal ArticleDOI
The DNA Damage Response: Ten Years After
TL;DR: This work has witnessed an explosion in understanding of DNA damage sensing, signaling, and the complex interplay between protein phosphorylation and the ubiquitin pathway employed by the DDR network to execute the response to DNA damage.
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Mechanism of eukaryotic homologous recombination.
TL;DR: HR accessory factors that facilitate other stages of the Rad51- and Dmc1-catalyzed homologous DNA pairing and strand exchange reaction have also been identified.
Journal ArticleDOI
Regulation of DNA repair throughout the cell cycle
Dana Branzei,Marco Foiani +1 more
TL;DR: The repair of DNA lesions that occur endogenously or in response to diverse genotoxic stresses is indispensable for genome integrity and has provided insights into the mechanisms that contribute to DNA repair in specific cell-cycle phases.
Journal ArticleDOI
Hydroxyurea-Stalled Replication Forks Become Progressively Inactivated and Require Two Different RAD51-Mediated Pathways for Restart and Repair
Eva Petermann,Manuel Luis Orta,Manuel Luis Orta,Natalia Issaeva,Niklas Schultz,Thomas Helleday,Thomas Helleday +6 more
TL;DR: The XRCC3 protein, which is required for RAD51 foci formation, is also required for replication restart of HU-stalled forks, suggesting that RAD51-mediated strand invasion supports fork restart.
References
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Journal ArticleDOI
SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
TL;DR: It is shown by genetic analysis that SUMO-modified PCNA functionally cooperates with Srs2, a helicase that blocks recombinational repair by disrupting Rad51 nucleoprotein filaments, which suggests a model in whichsumO- modified PCNA recruits SRS2 in S phase in order to prevent unwanted recombination events of replicating chromosomes.
Journal ArticleDOI
DNA helicase Srs2 disrupts the Rad51 presynaptic filament
Lumir Krejci,Stephen Van Komen,Ying Li,Jana Villemain,Mothe Sreedhar Reddy,Hannah L. Klein,Thomas E. Ellenberger,Patrick Sung +7 more
TL;DR: The role of SRS2 in recombination modulation is clarified by purifying its encoded product and examining its interactions with the Rad51 recombinase, and it is shown that Srs2 acts by dislodging Rad51 from ssDNA.
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Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast.
TL;DR: Sgs1 and its associated topoisomerase Top3 remove double Holliday junction intermediates from a crossover-producing repair pathway, thereby reducing crossovers and Srs2 promotes the noncrossover synthesis-dependent strand-annealing pathway, apparently by regulating Rad51 binding during strand exchange.
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The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments.
Xavier Veaute,Josette Jeusset,Christine Soustelle,Stephen C. Kowalczykowski,Eric Le Cam,Francis Fabre +5 more
TL;DR: It is shown that DNA strand exchange mediated in vitro by Rad51 is inhibited by Srs2, and that SRS2 disrupts Rad51 filaments formed on single-stranded DNA, providing an explanation for the anti-recombinogenic role of Srs1 in vivo and highlighting a previously unknown mechanism for recombination control.
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A ubiquitin mutant with specific defects in DNA repair and multiubiquitination.
TL;DR: The results of this study suggest that Lys-63 is used as a linkage site in the formation of novel multiubiquitin chain structures that play an important role in DNA repair.
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