Relevant bibliographies by topics / DNA damage checkpoint

Academic literature on the topic 'DNA damage checkpoint'

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Published: 4 June 2021
Last updated: 10 March 2023

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Journal articles on the topic "DNA damage checkpoint"

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Heideker, Johanna, Ewa T. Lis, and Floyd E. Romesberg. "Phosphatases, DNA Damage Checkpoints and Checkpoint Deactivation." Cell Cycle 6, no. 24 (December 15, 2007): 3058–64. http://dx.doi.org/10.4161/cc.6.24.5100.

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Bashkirov, Vladimir I., Jeff S. King, Elena V. Bashkirova, Jacqueline Schmuckli-Maurer, and Wolf-Dietrich Heyer. "DNA Repair Protein Rad55 Is a Terminal Substrate of the DNA Damage Checkpoints." Molecular and Cellular Biology 20, no. 12 (June 15, 2000): 4393–404. http://dx.doi.org/10.1128/mcb.20.12.4393-4404.2000.

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ABSTRACT Checkpoints, which are integral to the cellular response to DNA damage, coordinate transient cell cycle arrest and the induced expression of DNA repair genes after genotoxic stress. DNA repair ensures cellular survival and genomic stability, utilizing a multipathway network. Here we report evidence that the two systems, DNA damage checkpoint control and DNA repair, are directly connected by demonstrating that the Rad55 double-strand break repair protein of the recombinational repair pathway is a terminal substrate of DNA damage and replication block checkpoints. Rad55p was specifically phosphorylated in response to DNA damage induced by the alkylating agent methyl methanesulfonate, dependent on an active DNA damage checkpoint. Rad55p modification was also observed after gamma ray and UV radiation. The rapid time course of phosphorylation and the recombination defects identified in checkpoint-deficient cells are consistent with a role of the DNA damage checkpoint in activating recombinational repair. Rad55p phosphorylation possibly affects the balance between different competing DNA repair pathways.
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Stokes, Matthew P., Ruth Van Hatten, Howard D. Lindsay, and W. Matthew Michael. "DNA replication is required for the checkpoint response to damaged DNA in Xenopus egg extracts." Journal of Cell Biology 158, no. 5 (September 2, 2002): 863–72. http://dx.doi.org/10.1083/jcb.200204127.

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Alkylating agents, such as methyl methanesulfonate (MMS), damage DNA and activate the DNA damage checkpoint. Although many of the checkpoint proteins that transduce damage signals have been identified and characterized, the mechanism that senses the damage and activates the checkpoint is not yet understood. To address this issue for alkylation damage, we have reconstituted the checkpoint response to MMS in Xenopus egg extracts. Using four different indicators for checkpoint activation (delay on entrance into mitosis, slowing of DNA replication, phosphorylation of the Chk1 protein, and physical association of the Rad17 checkpoint protein with damaged DNA), we report that MMS-induced checkpoint activation is dependent upon entrance into S phase. Additionally, we show that the replication of damaged double-stranded DNA, and not replication of damaged single-stranded DNA, is the molecular event that activates the checkpoint. Therefore, these data provide direct evidence that replication forks are an obligate intermediate in the activation of the DNA damage checkpoint.
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Iyer, Divya Ramalingam, and Nicholas Rhind. "Checkpoint regulation of replication forks: global or local?" Biochemical Society Transactions 41, no. 6 (November 20, 2013): 1701–5. http://dx.doi.org/10.1042/bst20130197.

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Cell-cycle checkpoints are generally global in nature: one unattached kinetochore prevents the segregation of all chromosomes; stalled replication forks inhibit late origin firing throughout the genome. A potential exception to this rule is the regulation of replication fork progression by the S-phase DNA damage checkpoint. In this case, it is possible that the checkpoint is global, and it slows all replication forks in the genome. However, it is also possible that the checkpoint acts locally at sites of DNA damage, and only slows those forks that encounter DNA damage. Whether the checkpoint regulates forks globally or locally has important mechanistic implications for how replication forks deal with damaged DNA during S-phase.
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Audry, Julien, Jinyu Wang, Jessica R. Eisenstatt, Kathleen L. Berkner, and Kurt W. Runge. "The inhibition of checkpoint activation by telomeres does not involve exclusion of dimethylation of histone H4 lysine 20 (H4K20me2)." F1000Research 7 (October 9, 2018): 1027. http://dx.doi.org/10.12688/f1000research.15166.2.

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DNA double-strand breaks (DSBs) activate the DNA damage checkpoint machinery to pause or halt the cell cycle. Telomeres, the specific DNA-protein complexes at linear eukaryotic chromosome ends, are capped DSBs that do not activate DNA damage checkpoints. This “checkpoint privileged” status of telomeres was previously investigated in the yeast Schizosaccharomyces pombelacking the major double-stranded telomere DNA binding protein Taz1. Telomeric DNA repeats in cells lacking Taz1 are 10 times longer than normal and contain single-stranded DNA regions. DNA damage checkpoint proteins associate with these damaged telomeres, but the DNA damage checkpoint is not activated. This severing of the DNA damage checkpoint signaling pathway was reported to stem from exclusion of histone H4 lysine 20 dimethylation (H4K20me2) from telomeric nucleosomes in both wild type cells and cells lacking Taz1. However, experiments to identify the mechanism of this exclusion failed, prompting our re-evaluation of H4K20me2 levels at telomeric chromatin. In this short report, we used an extensive series of controls to identify an antibody specific for the H4K20me2 modification and show that the level of this modification is the same at telomeres and internal loci in both wild type cells and those lacking Taz1. Consequently, telomeres must block activation of the DNA Damage Response by another mechanism that remains to be determined.
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Garber, Peter M., and Jasper Rine. "Overlapping Roles of the Spindle Assembly and DNA Damage Checkpoints in the Cell-Cycle Response to Altered Chromosomes in Saccharomyces cerevisiae." Genetics 161, no. 2 (June 1, 2002): 521–34. http://dx.doi.org/10.1093/genetics/161.2.521.

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Abstract The MAD2-dependent spindle checkpoint blocks anaphase until all chromosomes have achieved successful bipolar attachment to the mitotic spindle. The DNA damage and DNA replication checkpoints block anaphase in response to DNA lesions that may include single-stranded DNA and stalled replication forks. Many of the same conditions that activate the DNA damage and DNA replication checkpoints also activated the spindle checkpoint. The mad2Δ mutation partially relieved the arrest responses of cells to mutations affecting the replication proteins Mcm3p and Pol1p. Thus a previously unrecognized aspect of spindle checkpoint function may be to protect cells from defects in DNA replication. Furthermore, in cells lacking either the DNA damage or the DNA replication checkpoints, the spindle checkpoint contributed to the arrest responses of cells to the DNA-damaging agent methyl methanesulfonate, the replication inhibitor hydroxyurea, and mutations affecting Mcm2p and Orc2p. Thus the spindle checkpoint was sensitive to a wider range of chromosomal perturbations than previously recognized. Finally, the DNA replication checkpoint did not contribute to the arrests of cells in response to mutations affecting ORC, Mcm proteins, or DNA polymerase δ. Thus the specificity of this checkpoint may be more limited than previously recognized.
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Rhind, Nicholas, and Paul Russell. "The Schizosaccharomyces pombe S-Phase Checkpoint Differentiates Between Different Types of DNA Damage." Genetics 149, no. 4 (August 1, 1998): 1729–37. http://dx.doi.org/10.1093/genetics/149.4.1729.

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Abstract We have identified an S-phase DNA damage checkpoint in Schizosaccharomyces pombe. This checkpoint is dependent on Rad3, the S. pombe homolog of the mammalian ATM/ATR checkpoint proteins, and Cds1. Cds1 had previously been believed to be involved only in the replication checkpoint. The requirement of Cds1 in the DNA damage checkpoint suggests that Cds1 may be a general target of S-phase checkpoints. Unlike other checkpoints, the S. pombe S-phase DNA damage checkpoint discriminates between different types of damage. UV-irradiation, which causes base modification that can be repaired during G1 and S-phase, invokes the checkpoint, while γ-irradiation, which causes double-stranded breaks that cannot be repaired by a haploid cell if induced before replication, does not invoke the checkpoint. Because the same genes are required to respond to UV- and γ-irradiation during G2, this discrimination may represent an active suppression of the γ response during S-phase.
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Paciotti, Vera, Michela Clerici, Maddalena Scotti, Giovanna Lucchini, and Maria Pia Longhese. "Characterization of mec1Kinase-Deficient Mutants and of New Hypomorphic mec1Alleles Impairing Subsets of the DNA Damage Response Pathway." Molecular and Cellular Biology 21, no. 12 (June 15, 2001): 3913–25. http://dx.doi.org/10.1128/mcb.21.12.3913-3925.2001.

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ABSTRACT DNA damage checkpoints lead to the inhibition of cell cycle progression following DNA damage. The Saccharomyces cerevisiae Mec1 checkpoint protein, a phosphatidylinositol kinase-related protein, is required for transient cell cycle arrest in response to DNA damage or DNA replication defects. We show thatmec1 kinase-deficient (mec1kd) mutants are indistinguishable from mec1Δ cells, indicating that the Mec1 conserved kinase domain is required for all known Mec1 functions, including cell viability and proper DNA damage response. Mec1kd variants maintain the ability to physically interact with both Ddc2 and wild-type Mec1 and cause dominant checkpoint defects when overproduced in MEC1 cells, impairing the ability of cells to slow down S phase entry and progression after DNA damage in G1 or during S phase. Conversely, an excess of Mec1kd inMEC1 cells does not abrogate the G2/M checkpoint, suggesting that Mec1 functions required for response to aberrant DNA structures during specific cell cycle stages can be separable. In agreement with this hypothesis, we describe two new hypomorphic mec1 mutants that are completely defective in the G1/S and intra-S DNA damage checkpoints but properly delay nuclear division after UV irradiation in G2. The finding that these mutants, although indistinguishable frommec1Δ cells with respect to the ability to replicate a damaged DNA template, do not lose viability after UV light and methyl methanesulfonate treatment suggests that checkpoint impairments do not necessarily result in hypersensitivity to DNA-damaging agents.
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Audry, Julien, Jinyu Wang, Jessica R. Eisenstatt, Kathleen L. Berkner, and Kurt W. Runge. "The inhibition of checkpoint activation by telomeres does not involve exclusion of dimethylation of histone H4 lysine 20 (H4K20me2)." F1000Research 7 (July 9, 2018): 1027. http://dx.doi.org/10.12688/f1000research.15166.1.

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DNA double-strand (DSBs) breaks activate the DNA damage checkpoint machinery to pause or halt the cell cycle. Telomeres, the specific DNA-protein complexes at linear eukaryotic chromosome ends, are capped DSBs that do not activate DNA damage checkpoints. This “checkpoint privileged” status of telomeres was previously investigated in the yeast Schizosaccharomyces pombe lacking the major double-stranded telomere DNA binding protein Taz1. Telomeric DNA repeats in cells lacking Taz1 are 10 times longer than normal and contain single-stranded DNA regions. DNA damage checkpoint proteins associate with these damaged telomeres, but the DNA damage checkpoint is not activated. This severing of the DNA damage checkpoint signaling pathway was reported to stem from exclusion of histone H4 lysine 20 dimethylation (H4K20me2) from telomeric nucleosomes in both wild type cells and cells lacking Taz1. However, experiments to identify the mechanism of this exclusion failed, prompting our re-evaluation of H4K20me2 levels at telomeric chromatin. In this short report, we used an extensive series of controls to identify an antibody specific for the H4K20me2 modification and show that the level of this modification is the same at telomeres and internal loci in both wild type cells and those lacking Taz1. Consequently, telomeres must block activation of the DNA Damage Response by another mechanism that remains to be determined.
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Toh, G. W. L., and N. F. Lowndes. "Role of the Saccharomyces cerevisiae Rad9 protein in sensing and responding to DNA damage." Biochemical Society Transactions 31, no. 1 (February 1, 2003): 242–46. http://dx.doi.org/10.1042/bst0310242.

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Eukaryotic cells have evolved surveillance mechanisms, known as DNA-damage checkpoints, that sense and respond to genome damage. DNA-damage checkpoint pathways ensure co-ordinated cellular responses to DNA damage, including cell cycle delays and activation of repair mechanisms. RAD9, from Saccharomyces cerevisiae, was the first damage checkpoint gene to be identified, although its biochemical function remained unknown until recently. This review examines briefly work that provides significant insight into how Rad9 activates the checkpoint signalling kinase Rad53.
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Dissertations / Theses on the topic "DNA damage checkpoint"

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Little, Elizabeth J. "DNA damage sensors in the checkpoint response." Diss., The University of Arizona, 2003. http://hdl.handle.net/10150/289950.

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The DNA damage checkpoint response detects DNA damage and responds to the damage by promoting DNA repair, transcriptional regulation, and cell cycle arrest. Prior to the beginning of this dissertation the checkpoint sensor proteins in S. cerevisiae were identified as Ddc1, Mec3, Rad9, Rad17 and Rad24. However, none of the sensors had been shown to bind DNA directly, an anticipated function of checkpoint sensors. To characterize these proteins a biochemical approach was taken to test whether any of the checkpoint sensor proteins could detect DNA. The associated DNA binding properties of Rad24 and Rad9 were identified and characterized for the first time. Both of these checkpoint sensor proteins have an affinity for ssDNA, a common intermediate DNA structure of most DNA repair processes. In addition, the DNA damage checkpoint mutant protein Rad24-1 is defective for binding to ssDNA, suggesting that Rad24 DNA binding is required for its function in the checkpoint response. The potential exonuclease activity of Rad 17 tested using purified protein and various DNA substrates. This study was based on reports that the Rad 17 homolog Rec 1 from U. maydis is a 3'→5 ' DNA exonuclease, and genetic data that indicated that Rad 17 has a role in telomere degradation. Exonuclease assays with Rad17 protein preparations and ssDNA found an associated weak exonuclease that was not significantly above background levels. Conserved residues of Rad 17 thought to be required for exonuclease activity and checkpoint activity were mutated and studied for their affect on the DNA damage checkpoint. These studies imply that in addition to the region of Rad17 that is homologous to PCNA, the long carboxy-terminal region of Rad17 is also required for its checkpoint activity. Collectively, these studies suggest that the common DNA repair intermediate structure single-stranded DNA is recognized by multiple checkpoint sensor proteins to initiate the DNA damage checkpoint response. This suggests that the initiation of the checkpoint response is the recognition of a single DNA structure instead of the many different structures of primary DNA damage by free radicals, UV, γ-radiation, alklylation, double strand breaks, and base mismatches.
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Ho, Chui Chui. "Characterization of the regulation of p53 and checkpoint kinases in DNA integrity checkpoints /." View abstract or full-text, 2006. http://library.ust.hk/cgi/db/thesis.pl?BICH%202006%20HO.

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Searle, Jennifer. "The Role of PKA in the DNA Damage Checkpoint." University of Cincinnati / OhioLINK, 2005. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1123003066.

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On, Kin Fan. "The role of MAD2L1BP in the silencing of the spindle-assembly checkpoint and the DNA damage checkpoint /." View abstract or full-text, 2009. http://library.ust.hk/cgi/db/thesis.pl?BICH%202009%20ON.

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Carrassa, Laura. "Molecular mechanisms regulating the G2 checkpoint induced after DNA damage." Thesis, Open University, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.434262.

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COLOMBO, CHIARA VITTORIA. "New insights into the regulation of DNA end processing and DNA damage checkpoint." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2019. http://hdl.handle.net/10281/241167.

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L’integrità genomica è minacciata da danni al DNA che, se non adeguatamente riparati, si convertono in mutazioni, il cui accumulo causa instabilità genomica, una tipica caratteristica tumorale. Le cellule eucariotiche reagiscono ai danni attivando la risposta ai danni al DNA. Le rotture a doppia elica del DNA (DSB) sono tra i danni più pericolosi. In Saccharomyces cerevisiae i DSB sono principalmente riparati tramite ricombinazione omologa (HR), che sfrutta sequenze omologhe come stampo per riparare il danno. La HR necessita il processamento nucleolitico (resection) delle estremità del DSB così da generare code di DNA a singolo filamento (ssDNA). La resection inizia con un taglio endonucleolitico da parte del complesso MRX insieme a Sae2, mentre l’estensione della resection è eseguita dalle nucleasi Exo1 e Dna2. Il checkpoint da danno al DNA è una cascata di trasduzione del segnale che blocca il ciclo cellulare così che le cellule abbiano tempo sufficiente per riparare il danno. In S. cerevisiae il checkpoint è attivato dalle chinasi Tel1 e Mec1, ortologhe di ATM e ATR umane. Una volta attivate, Mec1 e Tel1 fosforilano diversi substrati, tra cui l’adattatore Rad9 e la chinasi effettrice Rad53, che amplificano il segnale. Sia la resection che il checkpoint devono essere finemente regolati per garantire una riparazione efficiente dei DSB, evitando di generare troppo ssDNA, e per coordinare la riparazione con la progressione del ciclo. In questa tesi di dottorato, abbiamo dimostrato un nuovo livello di regolazione della resection, basato sul controllo della quantità di Exo1 da parte della proteina che lega l’RNA (RBP) Npl3. Inoltre, abbiamo studiato il ruolo di Sae2 nella riparazione dei danni e nell’attivazione del checkpoint. Npl3 svolge un ruolo chiave nel metabolismo degli RNA ed è molto conservata nell’uomo. Poiché studi recenti mostrano forti connessioni tra metabolismo degli RNA e mantenimento dell’integrità genomica, abbiamo verificato se Npl3 fosse coinvolta nella risposta ai DSB. Abbiamo dimostrato che l’assenza di Npl3 provoca difetti nel processamento delle estremità del DSB. In particolare, Npl3 promuove la resection estesa, agendo nello stesso pathway di Exo1. Inoltre, sia l’assenza di Npl3 che l’inattivazione dei suoi domini di legame all’RNA causano una riduzione del livello di Exo1. Quindi, Npl3 promuove la resection estesa regolando EXO1 a livello dell’RNA. Infatti, in assenza di Npl3, abbiamo dimostrato la presenza di molecole di RNA di EXO1 non correttamente terminate. Questi dati, oltre al fatto che l’overespressione di EXO1 sopprime parzialmente il difetto di resection di cellule npl3Δ, suggeriscono che Npl3 partecipi alla regolazione della resection promuovendo la corretta biogenesi dell’mRNA di EXO1. Riguardo al secondo progetto, Sae2 promuove l’attività endonucleasica di MRX durante la resection e regola negativamente il checkpoint Tel1-dipendente. Infatti, Sae2 limita l’accumulo di MRX alla lesione, riducendo sia il reclutamento che l’attività di segnalazione di Tel1. Non è ancora chiaro come le funzioni di Sae2 nel promuovere la resistenza ai danni e nell’inibire il checkpoint siano collegate. Tramite screening genetico, abbiamo identificato il mutante sae2-ms che, come accade in assenza di Sae2, iperattiva il checkpoint Tel1-dipendente, aumentando il reclutamento ai DSB sia di MRX che di Tel1. A differenza della delezione di Sae2, Sae2-ms non causa difetti di resection né di tethering, e non provoca sensibilità agli agenti genotossici. Inoltre, Sae2-ms provoca iperattivazione di Tel1, ma non di Rad53. Infatti, l’assenza di Sae2, ma non la presenza di Sae2-ms, aumenta l’interazione tra Rad53 e Rad9. Questi dati dimostrano che Sae2 regola il checkpoint sia controllando la rimozione di MRX dai DSB che limitando l’interazione Rad53-Rad9, e che l’inibizione di Rad53 è la principale responsabile della resistenza ai danni promossa da Sae2.
Genomic integrity is threatened by DNA damage that, if not properly repaired, can be converted into mutations, whose accumulation leads to genomic instability, one of the hallmarks of cancer. Eukaryotic cells deal with DNA damage by activating DNA damage response. DNA double strand breaks (DSBs) are among the most dangerous DNA lesions. In Saccharomyces cerevisiae, DSBs are mainly repaired by Homologous Recombination (HR), which exploits a homologous sequence as a template to repair the damage. HR requires the DSB ends to be nucleolytically degraded in order to generate single-strand DNA (ssDNA) tails, in a process known as DSB end resection. Resection initiates with an endonucleolytic cleavage by the MRX complex together with Sae2, while resection extension is carried out by the nucleases Exo1 and Dna2. DNA damage checkpoint is a signal transduction cascade that halts the cell cycle in order to give cells sufficient time to repair the damage. In S. cerevisiae, DNA damage checkpoint is activated by the kinases Tel1 and Mec1, orthologues of human ATM and ATR. Once activated, Mec1 and Tel1 phosphorylate different substrates including the adaptor Rad9 and the effector kinase Rad53, which allow signal amplification. Both DNA end resection and DNA damage checkpoint must be finely regulated to ensure efficient DSB repair, avoiding excessive ssDNA generation, and to properly coordinate repair with cell cycle progression. In this PhD thesis, we provide evidences of a new level of resection regulation, based on the modulation of Exo1 amount by the RNA-binding protein (RBP) Npl3. We have also studied the role of Sae2 in DNA damage repair and checkpoint activation. Npl3 is a S. cerevisiae RBP, which plays a central role in RNA metabolism and is highly conserved from yeast to humans. Since emerging evidences support strong connections between RNA metabolism and genome integrity, we investigated if Npl3 was involved in DSB response. We demonstrated that the absence of Npl3 impairs the generation of long ssDNA tails at DSB ends. In particular, Npl3 promotes resection extension by acting in the same pathway of Exo1. Moreover, both the lack of Npl3 and the inactivation of its RNA-binding domains cause the reduction of Exo1 protein level. So, Npl3 promotes resection extension by regulating EXO1 at the RNA level. Indeed, we proved that the decrease of Exo1 level is due to the presence of not properly terminated EXO1 RNA species. These findings, together with the observation that EXO1 overexpression partially suppresses the resection defect of npl3Δ cells, suggest that Npl3 participates in DSB end resection regulation by promoting the proper biogenesis of EXO1 mRNA. Concerning the second PhD project, Sae2 promotes MRX endonucleolytic activity during resection and negatively regulates Tel1-dependent checkpoint response. Indeed, Sae2 limits MRX accumulation at the damage site, thus reducing Tel1 recruitment and its signalling activity. How Sae2 functions in supporting DNA damage resistance and in inhibiting the DNA damage checkpoint are connected is still unclear. From a genetic screen, we identified the sae2-ms mutant that, similarly to Sae2 absence, upregulates Tel1 signalling activity by increasing both MRX and Tel1 recruitment to the DSBs. However, unlike SAE2 deletion, Sae2-ms does not cause any resection or tethering defect, nor any sensitivity to genotoxic agents. Moreover, Sae2-ms induces Tel1 but not Rad53 hyperactivation. Indeed Sae2 absence, but not Sae2-ms presence, increases Rad53-Rad9 interaction. These data indicate that Sae2 regulates checkpoint activation both by controlling MRX removal from the DSBs and by limiting Rad53-Rad9 interaction and that Rad53 downregulation is the main responsible for Sae2-promoted DNA damage resistance. Altogether, our results allow to better understand the molecular mechanisms involved in the control of DNA damage response processes.
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Yin, Ling. "Activation of DNA Replication Initiation Checkpoint in Fission Yeast." Scholarly Repository, 2009. http://scholarlyrepository.miami.edu/oa_dissertations/194.

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In the fission yeast, Schizosacchromyces pombe, blocks to DNA replication elongation trigger the intra-S phase checkpoint that leads to the activation of the Cds1 kinase. Cds1 is required to both stabilize stalled replication forks and to prevent premature entry into mitosis. Interestingly, although Cds1 is essential to maintain the viability of mutants defective in DNA replication elongation, my study shows that mutants defective in DNA replication initiation require the Chk1 kinase, rather than Cds1. This suggests that failed initiation events can lead to activation of the DNA damage checkpoint independent of the intra-S phase checkpoint. This might result from reduced origin firing that leads to an increase in replication fork stalling or replication fork collapse that activates the G2 DNA damage checkpoint. I refer to the Chk1-dependent, Cds1-independent phenotype as the rid phenotype (for replication initiation defective). The data shows that Chk1 is active in rid mutants when grown under semi-permissive conditions, and rid mutant viability is dependent on the DNA damage checkpoint, and surprisingly Mrc1, an adaptor protein required for activation of Cds1. Mutations in Mrc1 that prevent activation of Cds1 have no effect on its ability to support rid mutant viability, suggesting that Mrc1 has a checkpoint-independent role in maintaining the viability of mutants defective in DNA replication initiation. Like Mrc1, Swi1 and Swi3 have been hypothesized as a part of the replication fork protection complex (RFPC). They are required for maintaining the viability of rid mutants, but are not essential for activation of Chk1 in response to failed initiation events. This suggests that Mrc1 in conjunction with Swi1 and Swi3 function in a similar pathway to alleviate replicative stress resulting from defects in DNA replication initiation. Using flow cytometry, I demonstrate that inhibition of DNA replication initiation has no significant impact on the duration of S phase, suggesting dormant origins might be activated in response to defects in DNA replication initiation. Fission yeast Rad22 is implicated in forming nuclear foci in response to damaged DNA. By tracking YFP-labeled Rad22, I screened for potential DNA damage in rid mutants grown at semi-permissive temperatures, and the results show that DNA damage occurs as the result of defects in DNA replication initiation. I also identified camptothecin, a DNA topoisomerase I inhibitor that can at low dose (2 µM) induce the rid phenotype, suggesting our assay (Chk1-dependent, Cds1-independent) can be used to screen small molecule inhibitors that interfere with the initiation step of DNA replication.
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Chahwan, Richard. "Analysis of the DNA damage checkpoint and of the cytokinesis machinery." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613310.

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Choi, Jun-Hyuk Sancar Aziz. "Reconstitution of a human ATR-mediated DNA damage checkpoint prespone [sic]." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2009. http://dc.lib.unc.edu/u?/etd,2460.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2009.
Title from electronic title page (viewed Sep. 3, 2009). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Biochemistry and Biophysics." Discipline: Biochemistry and Biophysics; Department/School: Medicine.
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Martinho, Rui Goncalo V. R. C. "Analysis of Rad3 and Chk1 checkpoint protein kinases." Thesis, University of Sussex, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.297946.

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Books on the topic "DNA damage checkpoint"

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Quinlan, R. Jason. A kinetic analysis of the DNA damage checkpoint in the cell cycle. Sudbury, Ont: Laurentian University, 1998.

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Williams, Christine Janet. DNA Damage checkpoints in the development of normal and neoplastic lymphocytes. 1999.

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Book chapters on the topic "DNA damage checkpoint"

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Hartwell, Leland, Amanda Paulovich, and David Tocyzki. "The DNA Damage Checkpoint." In Genomic Instability and Immortality in Cancer, 149–57. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5365-6_10.

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Koltovaya, Natalia. "Kinase Cascade of DNA Damage Checkpoint." In Genetics, Evolution and Radiation, 125–38. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-48838-7_11.

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Abraham, Robert T., and Thanos D. Halazonetis. "DNA Damage Checkpoint Signaling Pathways in Human Cancer." In Signaling Pathways in Cancer Pathogenesis and Therapy, 23–37. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4614-1216-8_3.

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Tapia-Alveal, Claudia, and Matthew J. O’Connell. "Methods for Studying the G2 DNA Damage Checkpoint in Mammalian Cells." In Cell Cycle Checkpoints, 23–31. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-273-1_3.

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Romanov, Vasily, Aruna Shukla, and Zhenyu Ju. "DNA Damage and Checkpoint Responses in Adult Stem Cells." In Else Kröner-Fresenius Symposia, 74–82. Basel: S. KARGER AG, 2014. http://dx.doi.org/10.1159/000366568.

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Kuang, Jian, and Ruoning Wang. "Mechanisms of G2 Phase Arrest in DNA Damage-Induced Checkpoint Response." In Checkpoint Controls and Targets in Cancer Therapy, 37–51. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-178-3_3.

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Kaina, Bernd, Wynand P. Roos, and Markus Christmann. "DNA Damage Response and the Balance Between Cell Survival and Cell Death." In Checkpoint Controls and Targets in Cancer Therapy, 95–108. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-178-3_7.

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Lee, Mong-Hong, Sai-Ching Jim Yeung, and Heng-Yin Yang. "Interplay of 14-3-3 Family of Proteins with DNA Damage-Regulated Molecules in Checkpoint Control." In Checkpoint Controls and Targets in Cancer Therapy, 69–80. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-178-3_5.

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Kleinhans, Karin N., and Martin D. Burkhalter. "DNA Damage, Checkpoint Responses, and Cell Cycle Control in Aging Stem Cells." In Else Kröner-Fresenius Symposia, 36–47. Basel: S. KARGER AG, 2012. http://dx.doi.org/10.1159/000338016.

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Sperka, Tobias, Kodandaramireddy Nalapareddy, and K. Lenhard Rudolph. "DNA Damage, Checkpoint Responses, and Cell Cycle Control in Aging Stem Cells." In Molecular Mechanisms of Adult Stem Cell Aging, 95–104. Basel: KARGER, 2010. http://dx.doi.org/10.1159/000312653.

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Conference papers on the topic "DNA damage checkpoint"

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Shen, Changxian, and Peter Houghton. "Abstract LB-192: DNA damage checkpoints control spindle assembly checkpoint by regulating Mad2." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-lb-192.

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Yu, Bing, William B. Dalton, and Vincent W. Yang. "Abstract 3890: Regulation of mediator of DNA damage checkpoint 1 (MDC1) during mitosis." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3890.

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Hayashi, Makoto T., and Jan Karlseder. "Abstract IA20: A telomere-dependent DNA damage checkpoint induced by prolonged mitotic arrest." In Abstracts: AACR Special Conference: Cancer Susceptibility and Cancer Susceptibility Syndromes; January 29-February 1, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.cansusc14-ia20.

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Hayashi, Makoto, Anthony Cesare, James Fitzpatrick, Eros Lazzerini Denchi, and Jan Karlseder. "Abstract SY23-02: A telomere-dependent DNA damage checkpoint induced by prolonged mitotic arrest." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-sy23-02.

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Warren, Nicholas, Jennifer Ditano, and Alan Eastman. "Abstract 4298: Targeting the DNA damage checkpoint kinase Chk1 induces multiple pathways of cytotoxicity." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4298.

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Nishida, Hiroshi, Kayoko Kawakami, Naoto Tatewaki, Masao Hirayama, Nobuo Ikekawa, and Tetsuya Konishi. "Abstract 2971: The modulation checkpoint signaling by natural products during the DNA damage response." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2971.

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Yeo, D., R. Jorissen, M. Nikfarjam, and P. Ferrao. "PO-508 A novel predictor for stratifying pancreatic cancer patients to DNA damage checkpoint inhibitors." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.1009.

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Smith, Charlotte, Danilo Cucchi, Amy Gibson, Kirsten Brooksbank, and Sarah Martin. "Identification of genetic determinants of DNA mismatch repair loss that predict response to immune checkpoint blockade." In The 1st International Electronic Conference on Cancers: Exploiting Cancer Vulnerability by Targeting the DNA Damage Response. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iecc2021-09195.

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Wigan, Matthew, Sandra Pavey, Kelly Brooks, Nichole Giles, Andrew Burgess, Rick Sturm, and Brian Gabrielli. "Abstract 4197: A DNA damage checkpoint response to unrepaired ultraviolet radiation-induced lesions which is defective in melanoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4197.

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Chiyoda, Tatsuyuki, Shinji Kuninaka, Kenta Masuda, Takatsune Shimizu, Yoshimi Arima, Daisuke Aoki, and Hideyuki Saya. "Abstract 562: The Hippo pathway component LATS1 phosphorylates MYPT1 to counteract PLK1 and regulate G2 DNA damage checkpoint." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-562.

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Reports on the topic "DNA damage checkpoint"

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Scott, Kenneth L., and Sharon E. Plon. Alternative DNA Damage Checkpoint Pathways in Eukaryotes. Fort Belvoir, VA: Defense Technical Information Center, April 2001. http://dx.doi.org/10.21236/ada396714.

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Li, Yi-Chen J. Alternative DNA Damage Checkpoint Pathways in Eukaryotes. Fort Belvoir, VA: Defense Technical Information Center, April 1999. http://dx.doi.org/10.21236/ada369305.

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Li, Yi-Chen. Alternative DNA Damage Checkpoint Pathways in Eukaryotes. Fort Belvoir, VA: Defense Technical Information Center, April 2000. http://dx.doi.org/10.21236/ada381190.

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Byun, Tony S. The Role of Replication in Activation of the DNA Damage Checkpoint. Fort Belvoir, VA: Defense Technical Information Center, March 2005. http://dx.doi.org/10.21236/ada436935.

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Van, Christopher. The Role of Replication in Activation of the DNA Damage Checkpoint. Fort Belvoir, VA: Defense Technical Information Center, March 2006. http://dx.doi.org/10.21236/ada449918.

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Nyberg, Kara A., and Ted A. Weinert. Analysis of Rad9 Functions; Roles in the Checkpoint Response, DNA Damage Processing, and Prevention of Genomic Instability. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada418042.

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Wang, Bin, and Stephan Elledge. Involvement of 53BP1, a p53 Binding Protein, in Chk2 Phosphorylation of p53 and DNA Damage Cell Cycle Checkpoints. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada426338.

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Wang, Bin, and Stephen J. Elledge. Involvement of 53BP1, a p43 Binding Protein, in Chk2 Phosphorylation of p53 and DNA Damage Cell Cycle Checkpoints. Fort Belvoir, VA: Defense Technical Information Center, May 2003. http://dx.doi.org/10.21236/ada417278.

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