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Artykuły w czasopismach na temat "Rad51 filament"
Ma, Emilie, Laurent Maloisel, Léa Le Falher, Raphaël Guérois i Eric Coïc. "Rad52 Oligomeric N-Terminal Domain Stabilizes Rad51 Nucleoprotein Filaments and Contributes to Their Protection against Srs2". Cells 10, nr 6 (11.06.2021): 1467. http://dx.doi.org/10.3390/cells10061467.
Pełny tekst źródłaMaloisel, Laurent, Emilie Ma, Jamie Phipps, Alice Deshayes, Stefano Mattarocci, Stéphane Marcand, Karine Dubrana i Eric Coïc. "Rad51 filaments assembled in the absence of the complex formed by the Rad51 paralogs Rad55 and Rad57 are outcompeted by translesion DNA polymerases on UV-induced ssDNA gaps". PLOS Genetics 19, nr 2 (7.02.2023): e1010639. http://dx.doi.org/10.1371/journal.pgen.1010639.
Pełny tekst źródłaSullivan, Meghan R., i Kara A. Bernstein. "RAD-ical New Insights into RAD51 Regulation". Genes 9, nr 12 (13.12.2018): 629. http://dx.doi.org/10.3390/genes9120629.
Pełny tekst źródłaBurgess, Rebecca C., Michael Lisby, Veronika Altmannova, Lumir Krejci, Patrick Sung i Rodney Rothstein. "Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo". Journal of Cell Biology 185, nr 6 (8.06.2009): 969–81. http://dx.doi.org/10.1083/jcb.200810055.
Pełny tekst źródłaLiu, Jie, Ludovic Renault, Xavier Veaute, Francis Fabre, Henning Stahlberg i Wolf-Dietrich Heyer. "Rad51 paralogues Rad55–Rad57 balance the antirecombinase Srs2 in Rad51 filament formation". Nature 479, nr 7372 (23.10.2011): 245–48. http://dx.doi.org/10.1038/nature10522.
Pełny tekst źródłaOsman, Fekret, Julie Dixon, Alexis R. Barr i Matthew C. Whitby. "The F-Box DNA Helicase Fbh1 Prevents Rhp51-Dependent Recombination without Mediator Proteins". Molecular and Cellular Biology 25, nr 18 (15.09.2005): 8084–96. http://dx.doi.org/10.1128/mcb.25.18.8084-8096.2005.
Pełny tekst źródłaFung, Cindy W., Gary S. Fortin, Shaun E. Peterson i Lorraine S. Symington. "The rad51-K191R ATPase-Defective Mutant Is Impaired forPresynaptic Filament Formation". Molecular and Cellular Biology 26, nr 24 (9.10.2006): 9544–54. http://dx.doi.org/10.1128/mcb.00599-06.
Pełny tekst źródłaLu, Chih-Hao, Hsin-Yi Yeh, Guan-Chin Su, Kentaro Ito, Yumiko Kurokawa, Hiroshi Iwasaki, Peter Chi i Hung-Wen Li. "Swi5–Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation". Proceedings of the National Academy of Sciences 115, nr 43 (8.10.2018): E10059—E10068. http://dx.doi.org/10.1073/pnas.1812753115.
Pełny tekst źródłaMuhammad, Ali Akbar, Clara Basto, Thibaut Peterlini, Josée Guirouilh-Barbat, Melissa Thomas, Xavier Veaute, Didier Busso i in. "Human RAD52 stimulates the RAD51-mediated homology search". Life Science Alliance 7, nr 3 (11.12.2023): e202201751. http://dx.doi.org/10.26508/lsa.202201751.
Pełny tekst źródłaSlupianek, Artur, Shuyue Ren i Tomasz Skorski. "Selective Anti-Leukemia Targeting of the Interaction Between BCR/ABL and Mammalian RecA Homologs". Blood 112, nr 11 (16.11.2008): 195. http://dx.doi.org/10.1182/blood.v112.11.195.195.
Pełny tekst źródłaRozprawy doktorskie na temat "Rad51 filament"
Dupont, Chloé. "Régulation de la formation des nucléofilaments Rad51 par les complexes de paralogues de Rad51 chez la levure Saccharomyces cerevisiae". Electronic Thesis or Diss., université Paris-Saclay, 2024. http://www.theses.fr/2024UPASL009.
Pełny tekst źródłaHomologous recombination (HR) is one of the major repair pathways for DNA damage such as double-strand breaks (DSBs). This pathway is also involved in restarting replication forks stalled by DNA lesion. A key step in this repair pathway involves the formation of nucleoprotein filaments formed by Rad51 recombinase on single-stranded DNA (ssDNA). These nucleofilaments are responsible for homology search and invasion of an intact DNA similar to the damaged DNA in order to use it as a template for repair synthesis. The formation of these nucleofilaments is tightly regulated. In the budding yeast Saccharomyces cerevisiae, the formation of Rad51 filaments is ensured by positive regulators such as the Rad52 mediator protein and the two complexes composed of Rad51 paralogue proteins, the Rad55-Rad57 complex and the SHU complex. They also play a role in protecting this nucleofilament from the negative regulator Srs2 by counterbalancing its disassembly effects. To gain a better understanding of the regulatory mechanism of the Rad51 nucleofilament, we need a more detailed understanding of the complex interactions between these multiple players. During my thesis, we aimed at determining the structure of Rad51 paralog complexes in association with Rad51 filaments. To do this, we combined a structural bioinformatics approach, based on sequence alignments and the published structure of Rad51, with yeast two-hybrid (Y2H) experiments. This strategy allowed us to build for the first time a model for the organisation of Rad51 paralog complexes, the Rad55-Rad57 and SHU complexes, in association with the Rad51 recombinase. This model was further validated by genetic analysis of mutations disrupting each interaction domain. In our model, Rad55-Rad57 adopts a similar structure than a dimer of Rad51 and it interacts only with the 5'-end of Rad51 filaments and only through the Rad57 subunit. Our genetic analyses suggest that the major role of the interaction between Rad55-Rad57 and Rad51 is to protect Rad51 filaments against the Srs2 translocase. On the other side of Rad55-Rad57, Rad55 interacts with the Csm2 subunit of the SHU complex through its N-terminal end. Interestingly, our genetic analyses revealed that SHU and the N-terminal end of Rad55 are dispensable for DSB repair. However, they are involved in the repair of UV-induced single-strand breaks. We propose that the SHU complex stabilizes the binding of Rad55-Rad57 on ssDNA gaps, thereby promoting enhanced stability of Rad51 filaments. Thus, Rad51 filaments would be more resistant to the destabilising activity of the Srs2 translocase and would allow HR to compete with alternative gap filling pathways involving error-prone translesion DNA polymerases. Our data allow us to propose a model for the installation of the Rad51 filament by paralog complexes, Rad55-Rad57 and SHU, in collaboration with Rad52
Amunugama, Ravindra Bandara. "Insights into Regulation of Human RAD51 Nucleoprotein Filament Activity During Homologous Recombination". The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1321984760.
Pełny tekst źródłaDisseau, Ludovic. "Etude de l'association et de la dynamique de filaments nucléoprotéiques Rad51-ADN individuels dans les pinces magnétiques". Paris 6, 2010. http://www.theses.fr/2010PA066622.
Pełny tekst źródłaEsta, Aline. "Rôles de Rad52 et de Srs2 dans la régulation de la recombinaison homologue chez Saccharomyces cerevisiae". Paris 6, 2013. http://www.theses.fr/2013PA066691.
Pełny tekst źródłaHomologous recombination (HR) is essential for double-strand break repair and participates in post-replication restart of stalled and collapsed replication forks. However, HR can lead to genome rearrangements and has to be strictly controlled. The budding yeast Srs2 is involved in the elimination of lethal intermediates formed by recombination proteins. To shed light on these intermediates, we searched for mutations that bypass the requirement of Srs2 in DNA repair without affecting HR. Remarkably, we isolated several alleles of RAD52, a gene that codes for the most central recombination protein in yeast. Interestingly, we observed that these mutants bypass the requirement for Srs2 without affecting DNA repair by HR. The genetic study of one of these mutants (rad52-L264P) showed that it specifically prevents the formation of unproductive Rad51 filaments before strand invasion, allowing us to define Srs2 substrates. The avoidance of toxic Rad51 filaments can also be overcome by stimulating Rad52 sumoylation. Further analysis showed that some of the mutated Rad52 proteins and the sumoylated form of Rad52 are characterized by a modified mediator activity. One of these mutants, rad52-P381S have lost its interaction with Rad51 without affecting HR. In this mutant, HR is strictly dependent on RAD55. However, Rad51 filaments are not formed in rad52Δ cells. Altogether these results show that Rad55 can assemble Rad51 filaments in coordination with Rad52, even though Rad52 cannot interact with Rad51. The study of these mutants will help to better understand how the mediators and helicases regulate the Rad51 filaments formation and its characteristics
Lin, Yu-Hsuan, i 林宇軒. "Investigating How Mouse RAD51 Filament Dynamics Regulated by SWI5-SFR1 Complex Using Optical Tweezers". Thesis, 2017. http://ndltd.ncl.edu.tw/handle/8s9wx8.
Pełny tekst źródła國立臺灣大學
化學研究所
105
Homologous recombination catalyzed by RAD51 recombinases is a crucial DNA repair pathway in eukaryotes. In the presence of ATP, RAD51 assembles on single-stranded DNA to form nucleoprotein filaments, and initiates homologous recombinational repair of DNA double-stranded breaks. The SWI5-SFR1 complex has been found to regulate RAD51 filament assembly and enhance strand exchange activity, but the detailed mechanism is not clear. Here we improved our home-built optical tweezers platform to 1 nm resolution, and utilized it to study the assembly and disassembly dynamics of mRAD51 filaments in the presence of SWI5-SFR1 complex. In the case of double-stranded DNA, mRAD51 assembly process is stimulated in the prescence of SWI5-SFR1, but the disassembly process is not affected. On the other hand, mRAD51 assembles onto single-stranded DNA with an enhanced rate in the prescence of SWI5-SFR1, and the disassembly process from ssDNA is suppressed by the SWI5-SFR1 complex. This indicates that the SWI5-SFR1 stabilization function happens in the mRAD51 nucleoprotein filament formation onto single-stranded DNA, while SWI5-SFR1 only alters the kext of double-stranded DNA filament formation, not kdis. These regulatory functions of SWI5-SFR1 imply not only efficient stabilization of mRAD51 nucleoprotein filament during strand exchange, but also offer efficient mRAD51 turnover once the reaction is completed.
Chu, Chia-Chieh, i 朱家杰. "The 5′-segment of Rad51 nucleoprotein filament is preferentially used for successful strand exchange process". Thesis, 2012. http://ndltd.ncl.edu.tw/handle/04548732607908655775.
Pełny tekst źródła國立臺灣大學
化學研究所
100
Rad51 recombinases in eukaryotes and RecA recombinases in prokaryotes play an essential role in repairing damaged DNA by the homologous recombinational repair pathway. Once assembled on single-stranded (ss) DNA, Rad51 nucleoprotein filaments mediate the pairing and strand exchange with the homologous sequence. Single-molecule tethered particle motion (TPM) experiments monitor the DNA length and topology change during biochemical processes, and allow us to study the mechanistic details of DNA recombination processes. In the Rad51 invading strand experiments, beads were labeled on the invading ssDNA with sequence homologous to the surface-anchored duplex DNA. When bead-labeled Rad51 nucleoprotein filaments first interacted with the surface-anchored DNA, the initial Brownian motion (BM) amplitude which was resulted from the combined length contribution of the Rad51 nucleoprotein filament and surface anchored duplex DNA can be detected. The initial Brownian motion provides information on the initial contact point of the Rad51 nucleoprotein filament as well as its polarity preference for the stable synapses formation. A sum of two-segment model successfully describes the distribution of initial BM values. For transient events, the synaptic complex formation initiated at random position with no end preference. For events that drive successfully into the final strand exchange product, 5′-end segment of Rad51 nucleoprotein filament was preferentially used. Our studies suggest that Rad51 nucleoprotein filaments carry out initial strand exchange in the 5′-to-3′ direction.
Šimandlová, Jitka. "Charakterizace antirekombinázové aktivity lidské FBH1 helikázy". Master's thesis, 2012. http://www.nusl.cz/ntk/nusl-307793.
Pełny tekst źródłaLan, Wei-Hsuan, i 藍偉瑄. "Studying the nucleation preference of DNA recombinases Dmc1 and Rad51 during nucleoprotein filament formation using a single molecule method". Thesis, 2019. http://ndltd.ncl.edu.tw/handle/emf39g.
Pełny tekst źródła國立臺灣大學
化學研究所
107
Dmc1 and Rad51 recombinases play important roles in the DNA double strand break repair. During the homologous recombination, recombinase binds to the resected damaged DNA to form a nucleoprotein filament, responsible for homology pairing and strand exchange. Rad51 and Dmc1 both exist in most eukaryotic cells, sharing similar amino acid sequences, structures and functions. However, Rad51 is expressed in both mitotic and meiotic cells, but Dmc1 is a meiosis-specific recombinase. The underlying mechanism of this differential requirement is unclear. Here, we utilized single-molecule tethered particle motion experiments to compare the kinetics of nucleoprotein filament assembly of Saccharomyces cerevisiae Rad51 and Dmc1. Nucleation on single-stranded DNA (ssDNA) is the rate-limiting step of the nucleoprotein filament assembly. We found distinct differences of these two recombinases: (1) ScRad51 and ScDmc1 have different nucleation preferences of DNA structures. (2) The nucleation rate of ScRad51 is much faster than ScDmc1, indicating that ScRad51 has better ssDNA binding affinity, and preferentially assembles on ssDNA. However, ScDmc1 preferentially nucleates on DNA substrates with duplex DNA/ssDNA junction containing a 3′-ssDNA overhang, as it allows filament extension from 5′-to-3′ direction. Same 5′ ds/ssDNA junction preference is also found in mouse DMC1, suggesting the general and important role of this nucleation site preference for the Dmc1 recombinase. Surprisingly, in the DNA substrates containing short discontinuous patches of ScRad51, ScDmc1 assembly is stimulated. Our data imply that the nucleation of ScDmc1 on ssDNA requires docking sites, such as duplex DNA/ssDNA junction or Rad51 binding on ssDNA. Higher ssDNA affinity of ScRad51 might offer the nucleation docking sites for ScDmc1 assembly during meiosis.
Części książek na temat "Rad51 filament"
Roy, Upasana, i Eric C. Greene. "Single-Stranded for Single-Molecule Visualization of Rad51-ssDNA Filament Dynamics". W Methods in Molecular Biology, 193–207. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1290-3_11.
Pełny tekst źródłaZhao, Lingyun, Jingfei Xu, Weixing Zhao, Patrick Sung i Hong-Wei Wang. "Determining the RAD51-DNA Nucleoprotein Filament Structure and Function by Cryo-Electron Microscopy". W Methods in Enzymology, 179–99. Elsevier, 2018. http://dx.doi.org/10.1016/bs.mie.2017.12.002.
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