Relevant bibliographies by topics / Rad51 filament

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Rad51 filament'

Author: Grafiati
Published: 7 July 2024
Last updated: 31 July 2025

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Journal articles on the topic "Rad51 filament"

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Ma, Emilie, Laurent Maloisel, Léa Le Falher, Raphaël Guérois, and Eric Coïc. "Rad52 Oligomeric N-Terminal Domain Stabilizes Rad51 Nucleoprotein Filaments and Contributes to Their Protection against Srs2." Cells 10, no. 6 (2021): 1467. http://dx.doi.org/10.3390/cells10061467.

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Homologous recombination (HR) depends on the formation of a nucleoprotein filament of the recombinase Rad51 to scan the genome and invade the homologous sequence used as a template for DNA repair synthesis. Therefore, HR is highly accurate and crucial for genome stability. Rad51 filament formation is controlled by positive and negative factors. In Saccharomyces cerevisiae, the mediator protein Rad52 catalyzes Rad51 filament formation and stabilizes them, mostly by counteracting the disruptive activity of the translocase Srs2. Srs2 activity is essential to avoid the formation of toxic Rad51 fil
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Maloisel, Laurent, Emilie Ma, Jamie Phipps, et al. "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, no. 2 (2023): e1010639. http://dx.doi.org/10.1371/journal.pgen.1010639.

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The bypass of DNA lesions that block replicative polymerases during DNA replication relies on DNA damage tolerance pathways. The error-prone translesion synthesis (TLS) pathway depends on specialized DNA polymerases that incorporate nucleotides in front of base lesions, potentially inducing mutagenesis. Two error-free pathways can bypass the lesions: the template switching pathway, which uses the sister chromatid as a template, and the homologous recombination pathway (HR), which also can use the homologous chromosome as template. The balance between error-prone and error-free pathways control
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Sullivan, Meghan R., and Kara A. Bernstein. "RAD-ical New Insights into RAD51 Regulation." Genes 9, no. 12 (2018): 629. http://dx.doi.org/10.3390/genes9120629.

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The accurate repair of DNA is critical for genome stability and cancer prevention. DNA double-strand breaks are one of the most toxic lesions; however, they can be repaired using homologous recombination. Homologous recombination is a high-fidelity DNA repair pathway that uses a homologous template for repair. One central HR step is RAD51 nucleoprotein filament formation on the single-stranded DNA ends, which is a step required for the homology search and strand invasion steps of HR. RAD51 filament formation is tightly controlled by many positive and negative regulators, which are collectively
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Burgess, Rebecca C., Michael Lisby, Veronika Altmannova, Lumir Krejci, Patrick Sung, and Rodney Rothstein. "Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo." Journal of Cell Biology 185, no. 6 (2009): 969–81. http://dx.doi.org/10.1083/jcb.200810055.

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Homologous recombination (HR), although an important DNA repair mechanism, is dangerous to the cell if improperly regulated. The Srs2 “anti-recombinase” restricts HR by disassembling the Rad51 nucleoprotein filament, an intermediate preceding the exchange of homologous DNA strands. Here, we cytologically characterize Srs2 function in vivo and describe a novel mechanism for regulating the initiation of HR. We find that Srs2 is recruited separately to replication and repair centers and identify the genetic requirements for recruitment. In the absence of Srs2 activity, Rad51 foci accumulate, and
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Liu, Jie, Ludovic Renault, Xavier Veaute, Francis Fabre, Henning Stahlberg, and Wolf-Dietrich Heyer. "Rad51 paralogues Rad55–Rad57 balance the antirecombinase Srs2 in Rad51 filament formation." Nature 479, no. 7372 (2011): 245–48. http://dx.doi.org/10.1038/nature10522.

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Osman, Fekret, Julie Dixon, Alexis R. Barr, and Matthew C. Whitby. "The F-Box DNA Helicase Fbh1 Prevents Rhp51-Dependent Recombination without Mediator Proteins." Molecular and Cellular Biology 25, no. 18 (2005): 8084–96. http://dx.doi.org/10.1128/mcb.25.18.8084-8096.2005.

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ABSTRACT A key step in homologous recombination is the loading of Rad51 onto single-stranded DNA to form a nucleoprotein filament that promotes homologous DNA pairing and strand exchange. Mediator proteins, such as Rad52 and Rad55-Rad57, are thought to aid filament assembly by overcoming an inhibitory effect of the single-stranded-DNA-binding protein replication protein A. Here we show that mediator proteins are also required to enable fission yeast Rad51 (called Rhp51) to function in the presence of the F-box DNA helicase Fbh1. In particular, we show that the critical function of Rad22 (an or
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Fung, Cindy W., Gary S. Fortin, Shaun E. Peterson, and Lorraine S. Symington. "The rad51-K191R ATPase-Defective Mutant Is Impaired forPresynaptic Filament Formation." Molecular and Cellular Biology 26, no. 24 (2006): 9544–54. http://dx.doi.org/10.1128/mcb.00599-06.

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ABSTRACT The nucleoprotein filament formed by Rad51 polymerization on single-stranded DNA is essential for homologous pairing and strand exchange. ATP binding is required for Rad51 nucleoprotein filament formation and strand exchange, but ATP hydrolysis is not required for these functions in vitro. Previous studies have shown that a yeast strain expressing the rad51-K191R allele is sensitive to ionizing radiation, suggesting an important role for ATP hydrolysis in vivo. The recruitment of Rad51-K191R to double-strand breaks is defective in vivo, and this phenotype can be suppressed by eliminat
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Lu, Chih-Hao, Hsin-Yi Yeh, Guan-Chin Su, et al. "Swi5–Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation." Proceedings of the National Academy of Sciences 115, no. 43 (2018): E10059—E10068. http://dx.doi.org/10.1073/pnas.1812753115.

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Eukaryotic Rad51 protein is essential for homologous-recombination repair of DNA double-strand breaks. Rad51 recombinases first assemble onto single-stranded DNA to form a nucleoprotein filament, required for function in homology pairing and strand exchange. This filament assembly is the first regulation step in homologous recombination. Rad51 nucleation is kinetically slow, and several accessory factors have been identified to regulate this step. Swi5–Sfr1 (S5S1) stimulates Rad51-mediated homologous recombination by stabilizing Rad51 nucleoprotein filaments, but the mechanism of stabilization
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Muhammad, Ali Akbar, Clara Basto, Thibaut Peterlini, et al. "Human RAD52 stimulates the RAD51-mediated homology search." Life Science Alliance 7, no. 3 (2023): e202201751. http://dx.doi.org/10.26508/lsa.202201751.

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Homologous recombination (HR) is a DNA repair mechanism of double-strand breaks and blocked replication forks, involving a process of homology search leading to the formation of synaptic intermediates that are regulated to ensure genome integrity. RAD51 recombinase plays a central role in this mechanism, supported by its RAD52 and BRCA2 partners. If the mediator function of BRCA2 to load RAD51 on RPA-ssDNA is well established, the role of RAD52 in HR is still far from understood. We used transmission electron microscopy combined with biochemistry to characterize the sequential participation of
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Slupianek, Artur, Shuyue Ren, and Tomasz Skorski. "Selective Anti-Leukemia Targeting of the Interaction Between BCR/ABL and Mammalian RecA Homologs." Blood 112, no. 11 (2008): 195. http://dx.doi.org/10.1182/blood.v112.11.195.195.

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Abstract We showed before that cells transformed by BCR/ABL and other fusion tyrosine kinases (FTKs) such as TEL/ABL, TEL/JAK2 and TEL/PDGFR, inducing chronic myeloproliferative disorders (MPDs), and CD34+ chronic myeloid leukemia (CML) stem/ progenitor cells from chronic phase (CML-CP) and blast crisis (CML-BC) contain an excess of DNA double-strand breaks (DSBs) induced by reactive oxygen species (ROS) and genotoxic stress [Blood, 2005; Cell Cycle, 2006; DNA Repair, 2006; Cancer Res., 2008]. Recent studies also revealed that CD34+CD38− CML-CP and CML-BC stem cellenriched populations seem to
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Dissertations / Theses on the topic "Rad51 filament"

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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.

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La recombinaison homologue (RH) est une des voies majeures de réparation des dommages de l'ADN telles que les cassures double brin (CDB). Cette voie est également impliquée dans le redémarrage des fourches de réplication bloquées à une lésion. Une étape clé de cette voie de réparation consiste en la formation de filaments nucléoprotéiques formés de la recombinase Rad51 sur de l'ADN simple brin (ADNsb). Ces nucléofilaments sont responsables de la recherche d'homologie et de l'invasion d'un ADN intact et semblable à l'ADN endommagé afin de l'utiliser comme matrice pour la synthèse réparatrice. L
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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.

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Disseau, 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.

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Dans cette thèse, nous avons étudié plusieurs aspects des interactions entre l’ADN et la protéine Rad51 humaine, qui est l’acteur clé du processus de recombinaison homologue eucaryote (échange de brins de séquences homologues entre deux molécules d’ADN). Cette protéine polymérise pour former des filaments nucléoprotéiques hélicoïdaux au sein desquels, dans leur conformation « canonique », l’ADN est surétiré et sous-enroulé. La technique de pinces magnétiques utilisée permet de manipuler un filament individuel en exerçant une force et une contrainte de surenroulement aux extrémités de la molécu
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Esta, 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.

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La recombinaison homologue (RH) est essentielle à la réparation des cassures double-brin de l'ADN, mais elle peut être une source d'instabilité génétique et doit être strictement contrôlée. Il a été montré chez la levure que certains intermédiaires de RH sont létaux et que l’hélicase Srs2 a pour fonction de les éliminer. Cet aspect de la toxicité de la RH est mal connu. J’ai montré au cours de ma thèse que les structures toxiques de RH induites par des agents génotoxiques ou par des blocages de réplication dans les cellules haploïdes sont des filaments nucléoprotéiques Rad51 probablement non f
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Lin, Yu-Hsuan, and 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.

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碩士<br>國立臺灣大學<br>化學研究所<br>105<br>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 dynam
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Chu, Chia-Chieh, and 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.

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碩士<br>國立臺灣大學<br>化學研究所<br>100<br>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, bead
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Šimandlová, Jitka. "Charakterizace antirekombinázové aktivity lidské FBH1 helikázy." Master's thesis, 2012. http://www.nusl.cz/ntk/nusl-307793.

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Homologous recombination (HR) is an essential mechanism for accurate repair of DNA double-strand breaks (DSBs). However, HR must be tightly controlled because excessive or unwanted HR events can lead to genome instability, which is a prerequisite for premature aging and cancer development. A critical step of HR is the loading of RAD51 molecules onto single-stranded DNA regions generated in the vicinity of the DSB, leading to the formation of a nucleoprotein filament. Several DNA helicases have been involved in the regulation of the HR process. One of these is human FBH1 (F-box DNA helicase 1)
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Lan, Wei-Hsuan, and 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.

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碩士<br>國立臺灣大學<br>化學研究所<br>107<br>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 utilize
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Book chapters on the topic "Rad51 filament"

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Roy, Upasana, and Eric C. Greene. "Single-Stranded for Single-Molecule Visualization of Rad51-ssDNA Filament Dynamics." In Methods in Molecular Biology. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1290-3_11.

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Zhao, Lingyun, Jingfei Xu, Weixing Zhao, Patrick Sung, and Hong-Wei Wang. "Determining the RAD51-DNA Nucleoprotein Filament Structure and Function by Cryo-Electron Microscopy." In Methods in Enzymology. Elsevier, 2018. http://dx.doi.org/10.1016/bs.mie.2017.12.002.

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