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of 54
pro vyhledávání: '"Steven J. Brill"'
Autor:
Ibtissam Talhaoui, Manuel Bernal, Janet R. Mullen, Hugo Dorison, Benoit Palancade, Steven J. Brill, Gerard Mazón
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nucleases are regulated during the cell cycle to control for crossover formation and maintain genome integrity. Here the authors reveal that the yeast Holliday junction resolvase Yen is a sumoylation target and it is regulated by the ubiquitin ligase
Externí odkaz:
https://doaj.org/article/3cfa65190830498d99dea1560cd9177b
Autor:
Minxing Li, Janet R. Mullen, Samuel F. Bunting, Mikel Zaratiegui, Pragati Sharma, Steven J. Brill
Publikováno v:
Genetics. 206:1807-1821
Sumoylation is required to repair protein-linked DNA damage, but its presence can limit the use of alternative repair pathways. Through a suppressor... Protein modification by the small ubiquitin-like modifier (SUMO) plays important roles in genome m
Autor:
Steven J. Brill, Lumir Krejci, Melita Chavdarova, Victoria Marini, Michael Lisby, Alexandra Sisakova, Dana Vigasova, Hana Sedlackova
Publikováno v:
Nucleic Acids Research
Chavdarova, M, Marini, V, Sisakova, A, Sedlackova, H, Vigasova, D, Brill, S J, Lisby, M & Krejci, L 2015, ' Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates ', Nucleic Acids Research, vol. 43, no. 7, pp. 3626-3642 . https://doi.org/10.1093/nar/gkv198
Chavdarova, M, Marini, V, Sisakova, A, Sedlackova, H, Vigasova, D, Brill, S J, Lisby, M & Krejci, L 2015, ' Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates ', Nucleic Acids Research, vol. 43, no. 7, pp. 3626-3642 . https://doi.org/10.1093/nar/gkv198
A variety of DNA lesions, secondary DNA structures or topological stress within the DNA template may lead to stalling of the replication fork. Recovery of such forks is essential for the maintenance of genomic stability. The structure-specific endonu
Autor:
Chi-Fu Chen, Steven J. Brill
Publikováno v:
DNA Repair. 22:137-146
BLM and WRN are members of the RecQ family of DNA helicases that act to suppress genome instability and cancer predisposition. In addition to a RecQ helicase domain, each of these proteins contains an N-terminal domain of approximately 500 amino acid
Autor:
Steven J. Brill, Virginie Faure, Marie-Noëlle Simon, Stéphane Coulon, Vincent Géli, Yves Corda, Eric Gilson, Pierre Luciano, Julia Bos
Publikováno v:
The EMBO Journal. 31:2034-2046
In Saccharomyces cerevisiae, the telomerase complex binds to chromosome ends and is activated in late S-phase through a process coupled to the progression of the replication fork. Here, we show that the single-stranded DNA-binding protein RPA (replic
Publikováno v:
Molecular and Cellular Biology. 30:3737-3748
Protein sumoylation plays an important but poorly understood role in controlling genome integrity. In Saccharomyces cerevisiae, the Slx5-Slx8 SUMO-targeted Ub ligase appears to be needed to ubiquitinate sumoylated proteins that arise in the absence o
Autor:
Steven J. Brill, Chi-Fu Chen
Publikováno v:
The EMBO Journal. 29:1713-1725
The gene mutated in Bloom's syndrome, BLM, encodes a member of the RecQ family of DNA helicases that is needed to suppress genome instability and cancer predisposition. BLM is highly conserved and all BLM orthologs, including budding yeast Sgs1, have
Publikováno v:
Nucleic Acids Research
BLM and WRN are members of the RecQ family of DNA helicases, and in humans their loss is associated with syndromes characterized by genome instability and cancer predisposition. As the only RecQ DNA helicase in the yeast Saccharomyces cerevisiae, Sgs
Autor:
Steven J. Brill, Janet R. Mullen
Publikováno v:
Journal of Biological Chemistry. 283:19912-19921
Protein sumoylation is a regulated process that is important for the health of human and yeast cells. In budding yeast, a subset of sumoylated proteins is targeted for ubiquitination by a conserved heterodimeric ubiquitin (Ub) ligase, Slx5–Slx8, wh
Publikováno v:
Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis. 625:1-19
Previous studies in yeast have suggested that the SGS1 DNA helicase or the Mus81-Mms4 structure-specific endonuclease is required to suppress the accumulation of lethal recombination intermediates during DNA replication. However, the structure of the