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Articoli di riviste sul tema "Rad51 filament"

Autore: Grafiati

Pubblicato: 7 luglio 2024

Ultima modifica: 19 luglio 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Subramanyam, Shyamal, Mohammed Ismail, Ipshita Bhattacharya, and Maria Spies. "Tyrosine phosphorylation stimulates activity of human RAD51 recombinase through altered nucleoprotein filament dynamics." Proceedings of the National Academy of Sciences 113, no. 41 (2016): E6045—E6054. http://dx.doi.org/10.1073/pnas.1604807113.

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The DNA strand exchange protein RAD51 facilitates the central step in homologous recombination, a process fundamentally important for accurate repair of damaged chromosomes, restart of collapsed replication forks, and telomere maintenance. The active form of RAD51 is a nucleoprotein filament that assembles on single-stranded DNA (ssDNA) at the sites of DNA damage. The c-Abl tyrosine kinase and its oncogenic counterpart BCR-ABL fusion kinase phosphorylate human RAD51 on tyrosine residues 54 and 315. We combined biochemical reconstitutions of the DNA strand exchange reactions with total internal

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12

Li, X., X. P. Zhang, J. A. Solinger, et al. "Rad51 and Rad54 ATPase activities are both required to modulate Rad51-dsDNA filament dynamics." Nucleic Acids Research 35, no. 12 (2007): 4124–40. http://dx.doi.org/10.1093/nar/gkm412.

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13

Mazina, Olga M., and Alexander V. Mazin. "Human Rad54 Protein Stimulates DNA Strand Exchange Activity of hRad51 Protein in the Presence of Ca2+." Journal of Biological Chemistry 279, no. 50 (2004): 52042–51. http://dx.doi.org/10.1074/jbc.m410244200.

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Rad51 and Rad54 proteins play a key role in homologous recombination in eukaryotes. Recently, we reported that Ca2+is requiredin vitrofor human Rad51 protein to form an active nucleoprotein filament that is important for the search of homologous DNA and for DNA strand exchange, two critical steps of homologous recombination. Here we find that Ca2+is also required for hRad54 protein to effectively stimulate DNA strand exchange activity of hRad51 protein. This finding identifies Ca2+as a universal cofactor of DNA strand exchange promoted by mammalian homologous recombination proteinsin vitro. We

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14

Zhang, Hongshan, Jeffrey M. Schaub, and Ilya J. Finkelstein. "RADX condenses single-stranded DNA to antagonize RAD51 loading." Nucleic Acids Research 48, no. 14 (2020): 7834–43. http://dx.doi.org/10.1093/nar/gkaa559.

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Abstract RADX is a mammalian single-stranded DNA-binding protein that stabilizes telomeres and stalled replication forks. Cellular biology studies have shown that the balance between RADX and Replication Protein A (RPA) is critical for DNA replication integrity. RADX is also a negative regulator of RAD51-mediated homologous recombination at stalled forks. However, the mechanism of RADX acting on DNA and its interactions with RPA and RAD51 are enigmatic. Using single-molecule imaging of the key proteins in vitro, we reveal that RADX condenses ssDNA filaments, even when the ssDNA is coated with

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15

Godin, Stephen K., Meghan R. Sullivan, and Kara A. Bernstein. "Novel insights into RAD51 activity and regulation during homologous recombination and DNA replication." Biochemistry and Cell Biology 94, no. 5 (2016): 407–18. http://dx.doi.org/10.1139/bcb-2016-0012.

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In this review we focus on new insights that challenge our understanding of homologous recombination (HR) and Rad51 regulation. Recent advances using high-resolution microscopy and single molecule techniques have broadened our knowledge of Rad51 filament formation and strand invasion at double-strand break (DSB) sites and at replication forks, which are one of most physiologically relevant forms of HR from yeast to humans. Rad51 filament formation and strand invasion is regulated by many mediator proteins such as the Rad51 paralogues and the Shu complex, consisting of a Shu2/SWS1 family member

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16

Kiianitsa, K., J. A. Solinger, and W. D. Heyer. "Terminal association of Rad54 protein with the Rad51-dsDNA filament." Proceedings of the National Academy of Sciences 103, no. 26 (2006): 9767–72. http://dx.doi.org/10.1073/pnas.0604240103.

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17

Conway, Adam B., Thomas W. Lynch, Ying Zhang, et al. "Crystal structure of a Rad51 filament." Nature Structural & Molecular Biology 11, no. 8 (2004): 791–96. http://dx.doi.org/10.1038/nsmb795.

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18

Cash, Kailey, and Maria Spies. "RAD51 filament formation, dynamics, and regulation." Biophysical Journal 122, no. 3 (2023): 355a. http://dx.doi.org/10.1016/j.bpj.2022.11.1968.

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19

Adolph, Madison, Swati Balakrishnan, Walter Chazin, and David Cortez. "Abstract IA024: Mechanistic insights into how RADX regulates RAD51 nucleoprotein filaments to maintain genome stability and control replication stress responses." Cancer Research 84, no. 1_Supplement (2024): IA024. http://dx.doi.org/10.1158/1538-7445.dnarepair24-ia024.

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Abstract RAD51 nucleoprotein filaments are central to maintaining genome stability, governing crucial processes like homology-directed double-strand break repair, replication fork reversal, and shielding replication forks from nucleases. The precise regulation of RAD51 filament formation and stability is critical for these functions, which suppress tumorigenesis and determine cellular responses to common cancer therapies. RADX is a pivotal regulator of RAD51 in the context of DNA replication, impacting replication fork reversal and fork stabilization. After identifying RADX as an RPA-related R

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20

Herzberg, Kristina, Vladimir I. Bashkirov, Michael Rolfsmeier, et al. "Phosphorylation of Rad55 on Serines 2, 8, and 14 Is Required for Efficient Homologous Recombination in the Recovery of Stalled Replication Forks." Molecular and Cellular Biology 26, no. 22 (2006): 8396–409. http://dx.doi.org/10.1128/mcb.01317-06.

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ABSTRACT DNA damage checkpoints coordinate the cellular response to genotoxic stress and arrest the cell cycle in response to DNA damage and replication fork stalling. Homologous recombination is a ubiquitous pathway for the repair of DNA double-stranded breaks and other checkpoint-inducing lesions. Moreover, homologous recombination is involved in postreplicative tolerance of DNA damage and the recovery of DNA replication after replication fork stalling. Here, we show that the phosphorylation on serines 2, 8, and 14 (S2,8,14) of the Rad55 protein is specifically required for survival as well

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21

Lan, Wei-Hsuan, Sheng-Yao Lin, Chih-Yuan Kao, et al. "Rad51 facilitates filament assembly of meiosis-specific Dmc1 recombinase." Proceedings of the National Academy of Sciences 117, no. 21 (2020): 11257–64. http://dx.doi.org/10.1073/pnas.1920368117.

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Dmc1 recombinases are essential to homologous recombination in meiosis. Here, we studied the kinetics of the nucleoprotein filament assembly ofSaccharomyces cerevisiaeDmc1 using single-molecule tethered particle motion experiments and in vitro biochemical assay. ScDmc1 nucleoprotein filaments are less stable than the ScRad51 ones because of the kinetically much reduced nucleation step. The lower nucleation rate of ScDmc1 results from its lower single-stranded DNA (ssDNA) affinity, compared to that of ScRad51. Surprisingly, ScDmc1 nucleates mostly on the DNA structure containing the single-stra

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22

Fornander, Louise H., Axelle Renodon-Cornière, Naoyuki Kuwabara, et al. "Swi5-Sfr1 protein stimulates Rad51-mediated DNA strand exchange reaction through organization of DNA bases in the presynaptic filament." Nucleic Acids Research 42, no. 4 (2013): 2358–65. http://dx.doi.org/10.1093/nar/gkt1257.

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Abstract The Swi5-Sfr1 heterodimer protein stimulates the Rad51-promoted DNA strand exchange reaction, a crucial step in homologous recombination. To clarify how this accessory protein acts on the strand exchange reaction, we have analyzed how the structure of the primary reaction intermediate, the Rad51/single-stranded DNA (ssDNA) complex filament formed in the presence of ATP, is affected by Swi5-Sfr1. Using flow linear dichroism spectroscopy, we observe that the nucleobases of the ssDNA are more perpendicularly aligned to the filament axis in the presence of Swi5-Sfr1, whereas the bases are

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23

Mazin, Alexander V., Carole J. Bornarth, Jachen A. Solinger, Wolf-Dietrich Heyer, and Stephen C. Kowalczykowski. "Rad54 Protein Is Targeted to Pairing Loci by the Rad51 Nucleoprotein Filament." Molecular Cell 6, no. 3 (2000): 583–92. http://dx.doi.org/10.1016/s1097-2765(00)00057-5.

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24

Bonilla, Braulio, Sarah R. Hengel, McKenzie K. Grundy, and Kara A. Bernstein. "RAD51 Gene Family Structure and Function." Annual Review of Genetics 54, no. 1 (2020): 25–46. http://dx.doi.org/10.1146/annurev-genet-021920-092410.

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Accurate DNA repair and replication are critical for genomic stability and cancer prevention. RAD51 and its gene family are key regulators of DNA fidelity through diverse roles in double-strand break repair, replication stress, and meiosis. RAD51 is an ATPase that forms a nucleoprotein filament on single-stranded DNA. RAD51 has the function of finding and invading homologous DNA sequences to enable accurate and timely DNA repair. Its paralogs, which arose from ancient gene duplications of RAD51, have evolved to regulate and promote RAD51 function. Underscoring its importance, misregulation of

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25

Colavito, S., M. Macris-Kiss, C. Seong, et al. "Functional significance of the Rad51-Srs2 complex in Rad51 presynaptic filament disruption." Nucleic Acids Research 37, no. 20 (2009): 6754–64. http://dx.doi.org/10.1093/nar/gkp748.

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26

Ogawa, T., X. Yu, A. Shinohara, and E. Egelman. "Similarity of the yeast RAD51 filament to the bacterial RecA filament." Science 259, no. 5103 (1993): 1896–99. http://dx.doi.org/10.1126/science.8456314.

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27

Chabot, Thomas, Alain Defontaine, Damien Marquis, et al. "New Phosphorylation Sites of Rad51 by c-Met Modulates Presynaptic Filament Stability." Cancers 11, no. 3 (2019): 413. http://dx.doi.org/10.3390/cancers11030413.

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Genomic instability through deregulation of DNA repair pathways can initiate cancer and subsequently result in resistance to chemo and radiotherapy. Understanding these biological mechanisms is therefore essential to overcome cancer. RAD51 is the central protein of the Homologous Recombination (HR) DNA repair pathway, which leads to faithful DNA repair of DSBs. The recombinase activity of RAD51 requires nucleofilament formation and is regulated by post-translational modifications such as phosphorylation. In the last decade, studies have suggested the existence of a relationship between recepto

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Jensen, Julia R., and Ryan B. Jensen. "Abstract 5603: Defining the functions of the BRCA2 BRC repeats in modulating RAD51 binding and activity." Cancer Research 84, no. 6_Supplement (2024): 5603. http://dx.doi.org/10.1158/1538-7445.am2024-5603.

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Abstract The BRCA2 (Breast Cancer Susceptibility 2) gene is critical for preserving genome integrity by regulating homology-directed repair (HDR) of DNA double-strand breaks (DSBs). Germline mutations in BRCA2 predispose individuals to a high risk for ovarian, breast, prostate, and pancreatic cancer. BRCA2 contains eight BRC repeats that mediate binding to RAD51. It remains unclear how exactly the different BRC repeats regulate RAD51 functions. In our study, we explore the importance of each BRC repeat, their interconnections, and their impact on RAD51 binding and filament stability. We engine

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29

Alexeev, Andrei, Alexander Mazin, and Stephen C. Kowalczykowski. "Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51–ssDNA nucleoprotein filament." Nature Structural & Molecular Biology 10, no. 3 (2003): 182–86. http://dx.doi.org/10.1038/nsb901.

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Krejci, Lumir, Stephen Van Komen, Ying Li, et al. "DNA helicase Srs2 disrupts the Rad51 presynaptic filament." Nature 423, no. 6937 (2003): 305–9. http://dx.doi.org/10.1038/nature01577.

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Amunugama, Ravindra, Yujiong He, Smaranda Willcox, et al. "RAD51 Protein ATP Cap Regulates Nucleoprotein Filament Stability." Journal of Biological Chemistry 287, no. 12 (2012): 8724–36. http://dx.doi.org/10.1074/jbc.m111.239426.

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32

Morrison, Ciaran, Akira Shinohara, Eiichiro Sonoda, et al. "The Essential Functions of Human Rad51 Are Independent of ATP Hydrolysis." Molecular and Cellular Biology 19, no. 10 (1999): 6891–97. http://dx.doi.org/10.1128/mcb.19.10.6891.

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ABSTRACT Genetic recombination and the repair of double-strand DNA breaks inSaccharomyces cerevisiae require Rad51, a homologue of theEscherichia coli RecA protein. In vitro, Rad51 binds DNA to form an extended nucleoprotein filament and catalyzes the ATP-dependent exchange of DNA between molecules with homologous sequences. Vertebrate Rad51 is essential for cell proliferation. Using site-directed mutagenesis of highly conserved residues of human Rad51 (hRad51) and gene targeting of the RAD51 locus in chicken DT40 cells, we examined the importance of Rad51’s highly conserved ATP-binding domain

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Shang, Yongliang, Tao Huang, Hongbin Liu, et al. "MEIOK21: a new component of meiotic recombination bridges required for spermatogenesis." Nucleic Acids Research 48, no. 12 (2020): 6624–39. http://dx.doi.org/10.1093/nar/gkaa406.

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Abstract Repair of DNA double-strand breaks (DSBs) with homologous chromosomes is a hallmark of meiosis that is mediated by recombination ‘bridges’ between homolog axes. This process requires cooperation of DMC1 and RAD51 to promote homology search and strand exchange. The mechanism(s) regulating DMC1/RAD51-ssDNA nucleoprotein filament and the components of ‘bridges’ remain to be investigated. Here we show that MEIOK21 is a newly identified component of meiotic recombination bridges and is required for efficient formation of DMC1/RAD51 foci. MEIOK21 dynamically localizes on chromosomes from on

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Peterson, Shaun E., Yinyin Li, Brian T. Chait, Max E. Gottesman, Richard Baer, and Jean Gautier. "Cdk1 uncouples CtIP-dependent resection and Rad51 filament formation during M-phase double-strand break repair." Journal of Cell Biology 194, no. 5 (2011): 705–20. http://dx.doi.org/10.1083/jcb.201103103.

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DNA double-strand break (DSB) resection, which results in RPA-bound single-stranded DNA (ssDNA), is activated in S phase by Cdk2. RPA-ssDNA activates the ATR-dependent checkpoint and homology-directed repair (HDR) via Rad51-dependent mechanisms. On the other hand, the fate of DSBs sustained during vertebrate M phase is largely unknown. We use cell-free Xenopus laevis egg extracts to examine the recruitment of proteins to chromatin after DSB formation. We find that S-phase extract recapitulates a two-step resection mechanism. M-phase chromosomes are also resected in cell-free extracts and cultu

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Taylor, Martin R. G., Mário Špírek, Chu Jian Ma, et al. "A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling." Molecular Cell 64, no. 5 (2016): 926–39. http://dx.doi.org/10.1016/j.molcel.2016.10.020.

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Petiot, Valentine, Charles I. White, and Olivier Da Ines. "DNA-binding site II is required for RAD51 recombinogenic activity inArabidopsis thaliana." Life Science Alliance 7, no. 8 (2024): e202402701. http://dx.doi.org/10.26508/lsa.202402701.

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Homologous recombination is a major pathway for the repair of DNA double strand breaks, essential both to maintain genomic integrity and to generate genetic diversity. Mechanistically, homologous recombination involves the use of a homologous DNA molecule as a template to repair the break. In eukaryotes, the search for and invasion of the homologous DNA molecule is carried out by two recombinases, RAD51 in somatic cells and RAD51 and DMC1 in meiotic cells. During recombination, the recombinases bind overhanging single-stranded DNA ends to form a nucleoprotein filament, which is the active spec

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37

Jamalruddin, Mohd Azrin, Emmanuel Tawiah, Isabela Contreras, McKenzie Grundy, and Kara Bernstein. "Abstract 1490: RAD51C-deficient cancer cells require DNA polymerase zeta to bypass cisplatin-induced lesion." Cancer Research 85, no. 8_Supplement_1 (2025): 1490. https://doi.org/10.1158/1538-7445.am2025-1490.

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RAD51C is a RAD51 paralog protein that mediates RAD51 filament formation on single-stranded DNA (ssDNA) in a canonical homologous recombination (HR) pathway. This step is vital for homology search to repair double strand breaks. RAD51C deficiency is linked to increased risks of developing breast and ovarian cancers. Fortunately, RAD51C-deficient cancer patients are generally responding well to chemotherapeutics drug like cisplatin. HR is one of the important pathways to repair cisplatin-induced lesion. Hence, cancer cells that lack RAD51C are more susceptible to cisplatin treatment. Nonetheles

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Martinez, Juan S., Catharina von Nicolai, Taeho Kim, et al. "BRCA2 regulates DMC1-mediated recombination through the BRC repeats." Proceedings of the National Academy of Sciences 113, no. 13 (2016): 3515–20. http://dx.doi.org/10.1073/pnas.1601691113.

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In somatic cells, BRCA2 is needed for RAD51-mediated homologous recombination. The meiosis-specific DNA strand exchange protein, DMC1, promotes the formation of DNA strand invasion products (joint molecules) between homologous molecules in a fashion similar to RAD51. BRCA2 interacts directly with both human RAD51 and DMC1; in the case of RAD51, this interaction results in stimulation of RAD51-promoted DNA strand exchange. However, for DMC1, little is known regarding the basis and functional consequences of its interaction with BRCA2. Here we report that human DMC1 interacts directly with each

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Adolph, Madison B., Taha M. Mohamed, Swati Balakrishnan, et al. "RADX controls RAD51 filament dynamics to regulate replication fork stability." Molecular Cell 81, no. 5 (2021): 1074–83. http://dx.doi.org/10.1016/j.molcel.2020.12.036.

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Lee, M., J. Lipfert, H. Sanchez, C. Wyman, and N. H. Dekker. "Structural and torsional properties of the RAD51-dsDNA nucleoprotein filament." Nucleic Acids Research 41, no. 14 (2013): 7023–30. http://dx.doi.org/10.1093/nar/gkt425.

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41

Qiu, Yupeng, Edwin Anthony, Timothy Lohman, and Sua Myong. "Srs2 Prevents Rad51 Filament Formation by Repetitive Scrunching of DNA." Biophysical Journal 104, no. 2 (2013): 75a. http://dx.doi.org/10.1016/j.bpj.2012.11.452.

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42

Candelli, Andrea, Jan T. Holhausen, Martin Depken, et al. "RAD51-Nucleoprotein Filament Assembly Quantified at the Single-Molecule Level." Biophysical Journal 104, no. 2 (2013): 369a. http://dx.doi.org/10.1016/j.bpj.2012.11.2049.

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43

Ma, Chu Jian, Bryan Gibb, YoungHo Kwon, Patrick Sung, and Eric C. Greene. "Protein dynamics of human RPA and RAD51 on ssDNA during assembly and disassembly of the RAD51 filament." Nucleic Acids Research 45, no. 2 (2016): 749–61. http://dx.doi.org/10.1093/nar/gkw1125.

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44

Galkin, Vitold E., Yan Wu, Xiao-Ping Zhang, et al. "The Rad51/RadA N-Terminal Domain Activates Nucleoprotein Filament ATPase Activity." Structure 14, no. 6 (2006): 983–92. http://dx.doi.org/10.1016/j.str.2006.04.001.

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45

Seong, Changhyun, Sierra Colavito, Youngho Kwon, Patrick Sung, and Lumir Krejci. "Regulation of Rad51 Recombinase Presynaptic Filament Assembly via Interactions with the Rad52 Mediator and the Srs2 Anti-recombinase." Journal of Biological Chemistry 284, no. 36 (2009): 24363–71. http://dx.doi.org/10.1074/jbc.m109.032953.

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46

Khade, Nilesh V., and Tomohiko Sugiyama. "Roles of C-Terminal Region of Yeast and Human Rad52 in Rad51-Nucleoprotein Filament Formation and ssDNA Annealing." PLOS ONE 11, no. 6 (2016): e0158436. http://dx.doi.org/10.1371/journal.pone.0158436.

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47

Seong, Changhyun, Sierra Colavito, Youngho Kwon, Patrick Sung, and Lumir Krejci. "Regulation of Rad51 recombinase presynaptic filament assembly via interactions with the Rad52 mediator and the Srs2 anti-recombinase." Journal of Biological Chemistry 287, no. 15 (2012): 12154. http://dx.doi.org/10.1074/jbc.a109.032953.

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48

Nifontova, Galina, Cathy Charlier, Nizar Ayadi, et al. "Photonic Crystal Surface Mode Real-Time Imaging of RAD51 DNA Repair Protein Interaction with the ssDNA Substrate." Biosensors 14, no. 1 (2024): 43. http://dx.doi.org/10.3390/bios14010043.

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Abstract (sommario):

Photonic crystals (PCs) are promising tools for label-free sensing in drug discovery screening, diagnostics, and analysis of ligand–receptor interactions. Imaging of PC surface modes has emerged as a novel approach to the detection of multiple binding events at the sensor surface. PC surface modification and decoration with recognition units yield an interface providing the highly sensitive detection of cancer biomarkers, antibodies, and oligonucleotides. The RAD51 protein plays a central role in DNA repair via the homologous recombination pathway. This recombinase is essential for the genome

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49

Bernstein, Kara A., Robert J. D. Reid, Ivana Sunjevaric, Kimberly Demuth, Rebecca C. Burgess, and Rodney Rothstein. "The Shu complex, which contains Rad51 paralogues, promotes DNA repair through inhibition of the Srs2 anti-recombinase." Molecular Biology of the Cell 22, no. 9 (2011): 1599–607. http://dx.doi.org/10.1091/mbc.e10-08-0691.

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Abstract (sommario):

The Shu complex, which contains RAD51 paralogues, is involved in the decision between homologous recombination and error-prone repair. We discovered a link to ribosomal DNA (rDNA) recombination when we found an interaction between one member of the Shu complex, SHU1, and UAF30, a component of the upstream activating factor complex (UAF), which regulates rDNA transcription. In the absence of Uaf30, rDNA copy number increases, and this increase depends on several functional subunits of the Shu complex. Furthermore, in the absence of Uaf30, we find that Shu1 and Srs2, an anti-recombinase DNA heli

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50

Slupianek, Artur, Yashodhara Dasgupta, Shu-yue Ren, Kimberly Cramer, and Tomasz Skorski. "Targeting Phosphotyrosine-315 In RAD51 Recombinase to Prevent BCR-ABL1 - Mediated Unfaithful Homeologous Recombination Repair." Blood 116, no. 21 (2010): 1190. http://dx.doi.org/10.1182/blood.v116.21.1190.1190.

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Abstract (sommario):

Abstract Abstract 1190 Background: CD34+ chronic myeloid leukemia (CML) stem/progenitor cells from chronic phase (CML-CP) and blast phase (CML-BP) and cell lines transformed by non-mutated BCR-ABL1 kinase or tyrosine kinase inhibitor (TKI)-resistant mutants contain numerous DNA double-strand breaks (DSBs) induced by reactive oxygen species (ROS) (Nowicki et al., Blood, 2006; Cramer et al., Cancer Res., 2008). DSBs may cause apoptosis if not repaired or chromosomal aberrations if repaired unfaithfully. We reported that numerous ROS and radiation induced DSBs generated chromosomal aberrations in

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