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Journal articles on the topic 'Fork reversal'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Liu, Wenpeng, Yuichiro Saito, Jessica Jackson, et al. "RAD51 bypasses the CMG helicase to promote replication fork reversal." Science 380, no. 6643 (2023): 382–87. http://dx.doi.org/10.1126/science.add7328.

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Replication fork reversal safeguards genome integrity as a replication stress response. DNA translocases and the RAD51 recombinase catalyze reversal. However, it remains unknown why RAD51 is required and what happens to the replication machinery during reversal. We find that RAD51 uses its strand exchange activity to circumvent the replicative helicase, which remains bound to the stalled fork. RAD51 is not required for fork reversal if the helicase is unloaded. Thus, we propose that RAD51 creates a parental DNA duplex behind the helicase that is used as a substrate by the DNA translocases for

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2

Sewilam, Reham S., Megan R. Reed, and Robert L. Eoff. "Abstract 1488: DNA polymerase kappa slows replication fork speed by promoting fork reversal in glioblastoma." Cancer Research 85, no. 8_Supplement_1 (2025): 1488. https://doi.org/10.1158/1538-7445.am2025-1488.

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Abstract Replication fork stalling in response to replication stress triggers the activation of replication stressresponse (RSR) pathways to facilitate repair and restart replication processes, including fork reversal andtranslesion DNA synthesis (TLS). During fork reversal, the replication fork undergoes a structural rearrangementto form a four-stranded structure, known as a “chicken foot, ” which helps regulate fork speed by recruitment ofdifferent fork reversal factors, including HLTF, and SMARCAL1. Optimal replication conditions ensure a relativelyconstant and rapid fork progression rate,

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3

Bhat, Kamakoti P., and David Cortez. "RPA and RAD51: fork reversal, fork protection, and genome stability." Nature Structural & Molecular Biology 25, no. 6 (2018): 446–53. http://dx.doi.org/10.1038/s41594-018-0075-z.

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4

Fierro-Fernandez, M., P. Hernandez, D. B. Krimer, A. Stasiak, and J. B. Schvartzman. "Topological locking restrains replication fork reversal." Proceedings of the National Academy of Sciences 104, no. 5 (2007): 1500–1505. http://dx.doi.org/10.1073/pnas.0609204104.

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5

Quinet, Annabel, Delphine Lemaçon, and Alessandro Vindigni. "Replication Fork Reversal: Players and Guardians." Molecular Cell 68, no. 5 (2017): 830–33. http://dx.doi.org/10.1016/j.molcel.2017.11.022.

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6

Thakar, Tanay, and George-Lucian Moldovan. "The emerging determinants of replication fork stability." Nucleic Acids Research 49, no. 13 (2021): 7224–38. http://dx.doi.org/10.1093/nar/gkab344.

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Abstract A universal response to replication stress is replication fork reversal, where the nascent complementary DNA strands are annealed to form a protective four-way junction allowing forks to avert DNA damage while replication stress is resolved. However, reversed forks are in turn susceptible to nucleolytic digestion of the regressed nascent DNA arms and rely on dedicated mechanisms to protect their integrity. The most well studied fork protection mechanism involves the BRCA pathway and its ability to catalyze RAD51 nucleofilament formation on the reversed arms of stalled replication fork

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7

Liu, W., A. Krishnamoorthy, R. Zhao, and D. Cortez. "Two replication fork remodeling pathways generate nuclease substrates for distinct fork protection factors." Science Advances 6, no. 46 (2020): eabc3598. http://dx.doi.org/10.1126/sciadv.abc3598.

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Fork reversal is a common response to replication stress, but it generates a DNA end that is susceptible to degradation. Many fork protection factors block degradation, but how they work remains unclear. Here, we find that 53BP1 protects forks from DNA2-mediated degradation in a cell type–specific manner. Fork protection by 53BP1 reduces S-phase DNA damage and hypersensitivity to replication stress. Unlike BRCA2, FANCD2, and ABRO1 that protect reversed forks generated by SMARCAL1, ZRANB3, and HLTF, 53BP1 protects forks remodeled by FBH1. This property is shared by the fork protection factors F

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8

Batenburg, Nicole L., Sofiane Y. Mersaoui, John R. Walker, et al. "Cockayne syndrome group B protein regulates fork restart, fork progression and MRE11-dependent fork degradation in BRCA1/2-deficient cells." Nucleic Acids Research 49, no. 22 (2021): 12836–54. http://dx.doi.org/10.1093/nar/gkab1173.

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Abstract Cockayne syndrome group B (CSB) protein has been implicated in the repair of a variety of DNA lesions that induce replication stress. However, little is known about its role at stalled replication forks. Here, we report that CSB is recruited to stalled forks in a manner dependent upon its T1031 phosphorylation by CDK. While dispensable for MRE11 association with stalled forks in wild-type cells, CSB is required for further accumulation of MRE11 at stalled forks in BRCA1/2-deficient cells. CSB promotes MRE11-mediated fork degradation in BRCA1/2-deficient cells. CSB possesses an intrins

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9

Torres, Rubén, Carolina Gándara, Begoña Carrasco, Ignacio Baquedano, Silvia Ayora, and Juan C. Alonso. "DisA Limits RecG Activities at Stalled or Reversed Replication Forks." Cells 10, no. 6 (2021): 1357. http://dx.doi.org/10.3390/cells10061357.

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The DNA damage checkpoint protein DisA and the branch migration translocase RecG are implicated in the preservation of genome integrity in reviving haploid Bacillus subtilis spores. DisA synthesizes the essential cyclic 3′, 5′-diadenosine monophosphate (c-di-AMP) second messenger and such synthesis is suppressed upon replication perturbation. In vitro, c-di-AMP synthesis is suppressed when DisA binds DNA structures that mimic stalled or reversed forks (gapped forks or Holliday junctions [HJ]). RecG, which does not form a stable complex with DisA, unwinds branched intermediates, and in the pres

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10

Le Masson, Marie, Zeynep Baharoglu, and Bénédicte Michel. "ruvAandruvBmutants specifically impaired for replication fork reversal." Molecular Microbiology 70, no. 2 (2008): 537–48. http://dx.doi.org/10.1111/j.1365-2958.2008.06431.x.

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11

De Septenville, Anne L., Stéphane Duigou, Hasna Boubakri, and Bénédicte Michel. "Replication Fork Reversal after Replication–Transcription Collision." PLoS Genetics 8, no. 4 (2012): e1002622. http://dx.doi.org/10.1371/journal.pgen.1002622.

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12

Zellweger, Ralph, Damian Dalcher, Karun Mutreja, et al. "Rad51-mediated replication fork reversal is a global response to genotoxic treatments in human cells." Journal of Cell Biology 208, no. 5 (2015): 563–79. http://dx.doi.org/10.1083/jcb.201406099.

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Replication fork reversal protects forks from breakage after poisoning of Topoisomerase 1. We here investigated fork progression and chromosomal breakage in human cells in response to a panel of sublethal genotoxic treatments, using other topoisomerase poisons, DNA synthesis inhibitors, interstrand cross-linking inducers, and base-damaging agents. We used electron microscopy to visualize fork architecture under these conditions and analyzed the association of specific molecular features with checkpoint activation. Our data identify replication fork uncoupling and reversal as global responses t

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13

Krishnamoorthy, Archana, Jessica Jackson, Taha Mohamed, Madison Adolph, Alessandro Vindigni, and David Cortez. "RADX prevents genome instability by confining replication fork reversal to stalled forks." Molecular Cell 81, no. 14 (2021): 3007–17. http://dx.doi.org/10.1016/j.molcel.2021.05.014.

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14

Thangavel, Saravanabhavan, Matteo Berti, Maryna Levikova, et al. "DNA2 drives processing and restart of reversed replication forks in human cells." Journal of Cell Biology 208, no. 5 (2015): 545–62. http://dx.doi.org/10.1083/jcb.201406100.

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Accurate processing of stalled or damaged DNA replication forks is paramount to genomic integrity and recent work points to replication fork reversal and restart as a central mechanism to ensuring high-fidelity DNA replication. Here, we identify a novel DNA2- and WRN-dependent mechanism of reversed replication fork processing and restart after prolonged genotoxic stress. The human DNA2 nuclease and WRN ATPase activities functionally interact to degrade reversed replication forks with a 5′-to-3′ polarity and promote replication restart, thus preventing aberrant processing of unresolved replicat

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15

Couch, Frank B., and David Cortez. "Fork reversal, too much of a good thing." Cell Cycle 13, no. 7 (2014): 1049–50. http://dx.doi.org/10.4161/cc.28212.

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16

Sogo, J. M. "Fork Reversal and ssDNA Accumulation at Stalled Replication Forks Owing to Checkpoint Defects." Science 297, no. 5581 (2002): 599–602. http://dx.doi.org/10.1126/science.1074023.

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17

Cotta-Ramusino, Cecilia, Daniele Fachinetti, Chiara Lucca, et al. "Exo1 Processes Stalled Replication Forks and Counteracts Fork Reversal in Checkpoint-Defective Cells." Molecular Cell 17, no. 1 (2005): 153–59. http://dx.doi.org/10.1016/j.molcel.2004.11.032.

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18

Jain, Chetan K., Swagata Mukhopadhyay, and Agneyo Ganguly. "RecQ Family Helicases in Replication Fork Remodeling and Repair: Opening New Avenues towards the Identification of Potential Targets for Cancer Chemotherapy." Anti-Cancer Agents in Medicinal Chemistry 20, no. 11 (2020): 1311–26. http://dx.doi.org/10.2174/1871520620666200518082433.

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Replication fork reversal and restart has gained immense interest as a central response mechanism to replication stress following DNA damage. Although the exact mechanism of fork reversal has not been elucidated precisely, the involvement of diverse pathways and different factors has been demonstrated, which are central to this phenomenon. RecQ helicases known for their vital role in DNA repair and maintaining genome stability has recently been implicated in the restart of regressed replication forks. Through interaction with vital proteins like Poly (ADP) ribose polymerase 1 (PARP1), these he

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19

Warren, Garrett, Richard Stein, Hassane Mchaourab, and Brandt Eichman. "Movement of the RecG Motor Domain upon DNA Binding Is Required for Efficient Fork Reversal." International Journal of Molecular Sciences 19, no. 10 (2018): 3049. http://dx.doi.org/10.3390/ijms19103049.

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RecG catalyzes reversal of stalled replication forks in response to replication stress in bacteria. The protein contains a fork recognition (“wedge”) domain that binds branched DNA and a superfamily II (SF2) ATPase motor that drives translocation on double-stranded (ds)DNA. The mechanism by which the wedge and motor domains collaborate to catalyze fork reversal in RecG and analogous eukaryotic fork remodelers is unknown. Here, we used electron paramagnetic resonance (EPR) spectroscopy to probe conformational changes between the wedge and ATPase domains in response to fork DNA binding by Thermo

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20

Grompone, Gianfranco, Dusko Ehrlich, and Bénédicte Michel. "Cells defective for replication restart undergo replication fork reversal." EMBO reports 5, no. 6 (2004): 607–12. http://dx.doi.org/10.1038/sj.embor.7400167.

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21

Atkinson, J., and P. McGlynn. "Replication fork reversal and the maintenance of genome stability." Nucleic Acids Research 37, no. 11 (2009): 3475–92. http://dx.doi.org/10.1093/nar/gkp244.

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22

Bhattacharjee, Somendra M. "Interfacial instability and DNA fork reversal by repair proteins." Journal of Physics: Condensed Matter 22, no. 15 (2010): 155102. http://dx.doi.org/10.1088/0953-8984/22/15/155102.

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23

Singleton, Martin R., Sarah Scaife, and Dale B. Wigley. "Structural Analysis of DNA Replication Fork Reversal by RecG." Cell 107, no. 1 (2001): 79–89. http://dx.doi.org/10.1016/s0092-8674(01)00501-3.

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24

Olavarrieta, L. "Supercoiling, knotting and replication fork reversal in partially replicated plasmids." Nucleic Acids Research 30, no. 3 (2002): 656–66. http://dx.doi.org/10.1093/nar/30.3.656.

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25

Graham, Ambassador Thomas, and Douglas B. Shaw. "Nearing a fork in the road: Proliferation or nuclear reversal?" Nonproliferation Review 6, no. 1 (1998): 70–76. http://dx.doi.org/10.1080/10736709808436736.

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26

Ray Chaudhuri, Arnab, Yoshitami Hashimoto, Raquel Herrador, et al. "Topoisomerase I poisoning results in PARP-mediated replication fork reversal." Nature Structural & Molecular Biology 19, no. 4 (2012): 417–23. http://dx.doi.org/10.1038/nsmb.2258.

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27

Chen, Bo-Ruei, Annabel Quinet, Andrea K. Byrum, et al. "XLF and H2AX function in series to promote replication fork stability." Journal of Cell Biology 218, no. 7 (2019): 2113–23. http://dx.doi.org/10.1083/jcb.201808134.

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XRCC4-like factor (XLF) is a non-homologous end joining (NHEJ) DNA double strand break repair protein. However, XLF deficiency leads to phenotypes in mice and humans that are not necessarily consistent with an isolated defect in NHEJ. Here we show that XLF functions during DNA replication. XLF undergoes cell division cycle 7–dependent phosphorylation; associates with the replication factor C complex, a critical component of the replisome; and is found at replication forks. XLF deficiency leads to defects in replication fork progression and an increase in fork reversal. The additional loss of H

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28

Khanduja, Jasbeer Singh, and K. Muniyappa. "Functional Analysis of DNA Replication Fork Reversal Catalyzed byMycobacterium tuberculosisRuvAB Proteins." Journal of Biological Chemistry 287, no. 2 (2011): 1345–60. http://dx.doi.org/10.1074/jbc.m111.304741.

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29

Neelsen, Kai J., and Massimo Lopes. "Replication fork reversal in eukaryotes: from dead end to dynamic response." Nature Reviews Molecular Cell Biology 16, no. 4 (2015): 207–20. http://dx.doi.org/10.1038/nrm3935.

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30

Amunugama, Ravindra, Smaranda Willcox, R. Alex Wu, et al. "Replication Fork Reversal during DNA Interstrand Crosslink Repair Requires CMG Unloading." Cell Reports 23, no. 12 (2018): 3419–28. http://dx.doi.org/10.1016/j.celrep.2018.05.061.

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31

Mutreja, Karun, Jana Krietsch, Jeannine Hess, et al. "ATR-Mediated Global Fork Slowing and Reversal Assist Fork Traverse and Prevent Chromosomal Breakage at DNA Interstrand Cross-Links." Cell Reports 24, no. 10 (2018): 2629–42. http://dx.doi.org/10.1016/j.celrep.2018.08.019.

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32

Mayle, Ryan, Lance Langston, Kelly R. Molloy, Dan Zhang, Brian T. Chait, and Michael E. O’Donnell. "Mcm10 has potent strand-annealing activity and limits translocase-mediated fork regression." Proceedings of the National Academy of Sciences 116, no. 3 (2018): 798–803. http://dx.doi.org/10.1073/pnas.1819107116.

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The 11-subunit eukaryotic replicative helicase CMG (Cdc45, Mcm2-7, GINS) tightly binds Mcm10, an essential replication protein in all eukaryotes. Here we show that Mcm10 has a potent strand-annealing activity both alone and in complex with CMG. CMG-Mcm10 unwinds and then reanneals single strands soon after they have been unwound in vitro. Given the DNA damage and replisome instability associated with loss of Mcm10 function, we examined the effect of Mcm10 on fork regression. Fork regression requires the unwinding and pairing of newly synthesized strands, performed by a specialized class of ATP

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33

Quinet, Annabel, Stephanie Tirman, Jessica Jackson, et al. "PRIMPOL-Mediated Adaptive Response Suppresses Replication Fork Reversal in BRCA-Deficient Cells." Molecular Cell 77, no. 3 (2020): 461–74. http://dx.doi.org/10.1016/j.molcel.2019.10.008.

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34

Guarino, Estrella, Israel Salguero, Alfonso Jiménez-Sánchez, and Elena C. Guzmán. "Double-Strand Break Generation under Deoxyribonucleotide Starvation in Escherichia coli." Journal of Bacteriology 189, no. 15 (2007): 5782–86. http://dx.doi.org/10.1128/jb.00411-07.

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ABSTRACT Stalled replication forks produced by three different ways of depleting deoxynucleoside triphosphate showed different capacities to undergo “replication fork reversal.” This reaction occurred at the stalled forks generated by hydroxyurea treatment, was impaired under thermal inactivation of ribonucleoside reductase, and did not take place under thymine starvation.

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35

Honda, Masayoshi, Emeleeta A. Paintsil, and Maria Spies. "RAD52 DNA Repair Protein is a Gatekeeper that Protects DNA Replication Forks from Regression by Fork Reversal Motors." Biophysical Journal 118, no. 3 (2020): 160a. http://dx.doi.org/10.1016/j.bpj.2019.11.988.

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36

Shao, Jieya, Mari Iwase, Rong Xu, and Shuyang Lin. "Abstract B017: VCP extracts the chromatin remodeler SNF2H from nascent DNA to stabilize stressed replication forks." Cancer Research 84, no. 1_Supplement (2024): B017. http://dx.doi.org/10.1158/1538-7445.dnarepair24-b017.

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Abstract Valosin-containing protein (VCP) is an evolutionarily conserved AAA+ ATPase which plays pleiotropic roles in global proteostasis by extracting polyubiquitinated proteins from various cellular organelles and structures and facilitating their turnover. Our recent work demonstrated that nuclear VCP activity during DNA damage response specifically depends on ATM/ATR/DNA-PK-mediated Ser784 phosphorylation. Ser784phosphorylation increases VCP ability to facilitate chromatin-associated protein degradation and is required for DNA repair, checkpoint signaling, and cell survival. Clinically, hi

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37

Saldanha, Joanne, Julie Rageul, Jinal A. Patel, and Hyungjin Kim. "The Adaptive Mechanisms and Checkpoint Responses to a Stressed DNA Replication Fork." International Journal of Molecular Sciences 24, no. 13 (2023): 10488. http://dx.doi.org/10.3390/ijms241310488.

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DNA replication is a tightly controlled process that ensures the faithful duplication of the genome. However, DNA damage arising from both endogenous and exogenous assaults gives rise to DNA replication stress associated with replication fork slowing or stalling. Therefore, protecting the stressed fork while prompting its recovery to complete DNA replication is critical for safeguarding genomic integrity and cell survival. Specifically, the plasticity of the replication fork in engaging distinct DNA damage tolerance mechanisms, including fork reversal, repriming, and translesion DNA synthesis,

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38

Cybulla, Emily, Jessica Jackson, Stephanie Tirman, Annabel Quinet, Delphine Lemacon, and Alessandro Vindigni. "Abstract 803: Identifying a RAD18/UBC13-dependent mechanism of replication fork recovery to modulate chemoresponse in BRCA1-deficient cancers." Cancer Research 82, no. 12_Supplement (2022): 803. http://dx.doi.org/10.1158/1538-7445.am2022-803.

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Abstract Mutations in the breast cancer susceptibility genes BRCA1 and BRCA2 are associated with an increased lifetime risk of breast and ovarian cancers. While the BRCA proteins play a well-established role in double-stranded DNA break repair, recent studies have revealed an emerging role of BRCA1/2 in replication stress response. While replication forks are extensively degraded by nucleases in BRCA-deficient cancer cells, activation of specialized fork recovery mechanisms enables resumption of DNA synthesis and promotes cell survival. My project aims to determine this fork recovery mechanism

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39

Follonier, Cindy, Judith Oehler, Raquel Herrador, and Massimo Lopes. "Friedreich's ataxia–associated GAA repeats induce replication-fork reversal and unusual molecular junctions." Nature Structural & Molecular Biology 20, no. 4 (2013): 486–94. http://dx.doi.org/10.1038/nsmb.2520.

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40

Fierro-Fernández, Marta, Pablo Hernández, Dora B. Krimer, and Jorge B. Schvartzman. "Replication Fork Reversal Occurs Spontaneously after Digestion but Is Constrained in Supercoiled Domains." Journal of Biological Chemistry 282, no. 25 (2007): 18190–96. http://dx.doi.org/10.1074/jbc.m701559200.

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41

Kile, Andrew C., Diana A. Chavez, Julien Bacal, et al. "HLTF’s Ancient HIRAN Domain Binds 3′ DNA Ends to Drive Replication Fork Reversal." Molecular Cell 58, no. 6 (2015): 1090–100. http://dx.doi.org/10.1016/j.molcel.2015.05.013.

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42

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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43

Flores, Maria Jose, Vladimir Bidnenko, and Bénédicte Michel. "The DNA repair helicase UvrD is essential for replication fork reversal in replication mutants." EMBO reports 5, no. 10 (2004): 983–88. http://dx.doi.org/10.1038/sj.embor.7400262.

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44

Dixit, Suruchi, Tarun Nagraj, Debanjali Bhattacharya, et al. "RTEL1 helicase counteracts RAD51-mediated homologous recombination and fork reversal to safeguard replicating genomes." Cell Reports 43, no. 8 (2024): 114594. http://dx.doi.org/10.1016/j.celrep.2024.114594.

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45

Tian, Tian, Min Bu, Xu Chen, et al. "The ZATT-TOP2A-PICH Axis Drives Extensive Replication Fork Reversal to Promote Genome Stability." Molecular Cell 81, no. 1 (2021): 198–211. http://dx.doi.org/10.1016/j.molcel.2020.11.007.

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46

Regairaz, Marie, Yong-Wei Zhang, Haiqing Fu, et al. "Mus81-mediated DNA cleavage resolves replication forks stalled by topoisomerase I–DNA complexes." Journal of Cell Biology 195, no. 5 (2011): 739–49. http://dx.doi.org/10.1083/jcb.201104003.

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Deoxyribonucleic acid (DNA) topoisomerases are essential for removing the supercoiling that normally builds up ahead of replication forks. The camptothecin (CPT) Top1 (topoisomerase I) inhibitors exert their anticancer activity by reversibly trapping Top1–DNA cleavage complexes (Top1cc’s) and inducing replication-associated DNA double-strand breaks (DSBs). In this paper, we propose a new mechanism by which cells avoid Top1-induced replication-dependent DNA damage. We show that the structure-specific endonuclease Mus81-Eme1 is responsible for generating DSBs in response to Top1 inhibition and f

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47

Neelsen, Kai J., Isabella M. Y. Zanini, Raquel Herrador, and Massimo Lopes. "Oncogenes induce genotoxic stress by mitotic processing of unusual replication intermediates." Journal of Cell Biology 200, no. 6 (2013): 699–708. http://dx.doi.org/10.1083/jcb.201212058.

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Oncogene-induced DNA replication stress activates the DNA damage response (DDR), a crucial anticancer barrier. DDR inactivation in these conditions promotes genome instability and tumor progression, but the underlying molecular mechanisms are elusive. We found that overexpression of both Cyclin E and Cdc25A rapidly slowed down replication forks and induced fork reversal, suggestive of increased topological stress. Surprisingly, these phenotypes, per se, are neither associated with chromosomal breakage nor with significant DDR activation. Oncogene-induced DNA breakage and DDR activation instead

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48

Walker, John R., and Xu-Dong Zhu. "Role of Cockayne Syndrome Group B Protein in Replication Stress: Implications for Cancer Therapy." International Journal of Molecular Sciences 23, no. 18 (2022): 10212. http://dx.doi.org/10.3390/ijms231810212.

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A variety of endogenous and exogenous insults are capable of impeding replication fork progression, leading to replication stress. Several SNF2 fork remodelers have been shown to play critical roles in resolving this replication stress, utilizing different pathways dependent upon the nature of the DNA lesion, location on the DNA, and the stage of the cell cycle, to complete DNA replication in a manner preserving genetic integrity. Under certain conditions, however, the attempted repair may lead to additional genetic instability. Cockayne syndrome group B (CSB) protein, a SNF2 chromatin remodel

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49

Guarino, Estrella, Alfonso Jiménez-Sánchez, and Elena C. Guzmán. "Defective Ribonucleoside Diphosphate Reductase Impairs Replication Fork Progression in Escherichia coli." Journal of Bacteriology 189, no. 9 (2007): 3496–501. http://dx.doi.org/10.1128/jb.01632-06.

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ABSTRACT The observed lengthening of the C period in the presence of a defective ribonucleoside diphosphate reductase has been assumed to be due solely to the low deoxyribonucleotide supply in the nrdA101 mutant strain. We show here that the nrdA101 mutation induces DNA double-strand breaks at the permissive temperature in a recB-deficient background, suggesting an increase in the number of stalled replication forks that could account for the slowing of replication fork progression observed in the nrdA101 strain in a Rec+ context. These DNA double-strand breaks require the presence of the Holl

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50

Bai, Gongshi, Chames Kermi, Henriette Stoy, et al. "HLTF Promotes Fork Reversal, Limiting Replication Stress Resistance and Preventing Multiple Mechanisms of Unrestrained DNA Synthesis." Molecular Cell 78, no. 6 (2020): 1237–51. http://dx.doi.org/10.1016/j.molcel.2020.04.031.

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