Academic literature on the topic 'Ubiquitinace PCNA'

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Journal articles on the topic "Ubiquitinace PCNA"

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Frampton, Jonathan, Anja Irmisch, Catherine M. Green, et al. "Postreplication Repair and PCNA Modification in Schizosaccharomyces pombe." Molecular Biology of the Cell 17, no. 7 (2006): 2976–85. http://dx.doi.org/10.1091/mbc.e05-11-1008.

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Ubiquitination of proliferating cell nuclear antigen (PCNA) plays a crucial role in regulating replication past DNA damage in eukaryotes, but the detailed mechanisms appear to vary in different organisms. We have examined the modification of PCNA in Schizosaccharomyces pombe. We find that, in response to UV irradiation, PCNA is mono- and poly-ubiquitinated in a manner similar to that in Saccharomyces cerevisiae. However in undamaged Schizosaccharomyces pombe cells, PCNA is ubiquitinated in S phase, whereas in S. cerevisiae it is sumoylated. Furthermore we find that, unlike in S. cerevisiae, mu
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Zhang, Sufang, Jennifer Chea, Xiao Meng, Yajing Zhou, Ernest Y. C. Lee, and Marietta Y. W. T. Lee. "PCNA is ubiquitinated by RNF8." Cell Cycle 7, no. 21 (2008): 3399–404. http://dx.doi.org/10.4161/cc.7.21.6949.

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Ramasubramanyan, Sharada, Stephane Coulon, Robert P. Fuchs, Alan R. Lehmann, and Catherine M. Green. "Ubiquitin-PCNA fusion as a mimic for mono-ubiquitinated PCNA in Schizosaccharomyces pombe." DNA Repair 9, no. 7 (2010): 777–84. http://dx.doi.org/10.1016/j.dnarep.2010.03.015.

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Park, Eunmi, Jung Min Kim, Benjamin Primack, et al. "Inactivation ofUaf1Causes Defective Homologous Recombination and Early Embryonic Lethality in Mice." Molecular and Cellular Biology 33, no. 22 (2013): 4360–70. http://dx.doi.org/10.1128/mcb.00870-13.

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The deubiquitinating enzyme heterodimeric complex USP1-UAF1 regulates the Fanconi anemia (FA) DNA repair pathway. Absence of this complex leads to increased cellular levels of ubiquitinated FANCD2 (FANCD2-Ub) and ubiquitinated PCNA (PCNA-Ub). Mice deficient in the catalytic subunit of the complex, USP1, exhibit an FA-like phenotype and have a cellular deficiency in homologous-recombination (HR) repair. Here, we have characterized mice deficient in the UAF1 subunit.Uaf1+/−mice were small at birth and exhibited reduced fertility, thus resemblingUsp1−/−mice. Unexpectedly, homozygousUaf1−/−embryos
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Eger, Silvia, Benoît Castrec, Ulrich Hübscher, Martin Scheffner, Marina Rubini, and Andreas Marx. "Generation of a Mono-ubiquitinated PCNA Mimic by Click Chemistry." ChemBioChem 12, no. 18 (2011): 2807–12. http://dx.doi.org/10.1002/cbic.201100444.

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Bi, Xiaohui, Laura R. Barkley, Damien M. Slater та ін. "Rad18 Regulates DNA Polymerase κ and Is Required for Recovery from S-Phase Checkpoint-Mediated Arrest". Molecular and Cellular Biology 26, № 9 (2006): 3527–40. http://dx.doi.org/10.1128/mcb.26.9.3527-3540.2006.

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ABSTRACT We have investigated mechanisms that recruit the translesion synthesis (TLS) DNA polymerase Polκ to stalled replication forks. The DNA polymerase processivity factor PCNA is monoubiquitinated and interacts with Polκ in cells treated with the bulky adduct-forming genotoxin benzo[a]pyrene dihydrodiol epoxide (BPDE). A monoubiquitination-defective mutant form of PCNA fails to interact with Polκ. Small interfering RNA-mediated downregulation of the E3 ligase Rad18 inhibits BPDE-induced PCNA ubiquitination and association between PCNA and Polκ. Conversely, overexpressed Rad18 induces PCNA
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Eger, Silvia, Benoît Castrec, Ulrich Hübscher, Martin Scheffner, Marina Rubini, and Andreas Marx. "Corrigendum: Generation of a Mono-ubiquitinated PCNA Mimic by Click Chemistry." ChemBioChem 12, no. 18 (2011): 2716. http://dx.doi.org/10.1002/cbic.201100736.

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Kupfer, Gary M., and Xiaoyong Chen. "Regulation of PCNA Mono-Ubiqutination by FANCD2 and Rad51 in Response to Hydroxyurea." Blood 120, no. 21 (2012): 2377. http://dx.doi.org/10.1182/blood.v120.21.2377.2377.

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Abstract Abstract 2377 FANCD2 is a key player in FA pathway. It has been shown that FANCD2 can interact with PCNA and with Rad18, the ubiquitin ligase responsible for PCNA mono-ubiquitination. The mono-ubiquitination of PCNA is very important for its function in translesion synthesis. We found that in response to DNA damage agent hyxdroxyurea (HU) the interaction of FANCD2 with Rad18 or Rad51, and the interaction of Rad51 with Rad18 or PCNA was enhanced. FANCD2 is required for increased interaction between Rad51 and Rad18 indicating that FANCD2, Rad51 and Rad18 form a complex in response to HU
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Kupfer, Gary M., and Xiaoyong Chen. "FANCD2 and RAD51 Regulate PCNA Monoubiquitination and Translesion Synthesis." Blood 122, no. 21 (2013): 3712. http://dx.doi.org/10.1182/blood.v122.21.3712.3712.

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Abstract FANCD2 is a key player in Fanconi anemia (FA) pathway. It has been shown that PCNA and Rad18 can interact with FANCD2 and regulate FANCD2 monoubiquitination. Rad18 is the E3 ubiquitin ligase responsible for PCNA monoubiquitination, which is critical for PCNA function in translesion synthesis (TLS). Previous work by us and others has shown that the FA pathway interacts with PCNA and RAD18. Even though FA cells demonstrate unequivocal sensitivity to crosslinkers such as mitomycin C (MMC), we find surprisingly that they are largely resistant to hydroxyurea (HU), except for cells containi
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Lee, Kyoo-young, Kailin Yang, Martin A. Cohn, Nilabja Sikdar, Alan D. D'Andrea, and Kyungjae Myung. "Human ELG1 Regulates the Level of Ubiquitinated Proliferating Cell Nuclear Antigen (PCNA) through Its Interactions with PCNA and USP1." Journal of Biological Chemistry 285, no. 14 (2010): 10362–69. http://dx.doi.org/10.1074/jbc.m109.092544.

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Dissertations / Theses on the topic "Ubiquitinace PCNA"

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Ramasubramanyan, Sharada. "The role of ubiquitinated PCNA in regulating post-replication repair in Schizosaccharomyces pombe." Thesis, University of Sussex, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.494925.

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Post-replication repair (PRR) mechanisms operate to either excise or bypass lesions in the DNA that can stall progression of the replication fork. An important step in PRR is the ubiquifmation of proliferating cell nuclear antigen (PCNA) that serves as the sliding clamp/processivity factor for the replicative polymerases during DNA replication. It has been previously reported that monoubiquitinated PCNA has increased affinity for the TLS polymerases and hence, can stimulate the activity of the polymerases to by-pass replication stalling lesions (translesion synthesis) in the DNA.
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Schmutz, Valérie. "Réplication de l’ADN endommagé chez les eucaryotes : régulation et rôle de la mono-ubiquitination de PCNA." Strasbourg, 2010. http://www.theses.fr/2010STRA6045.

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Le génome des cellules est constamment soumis à des agressions exogènes ou endogènes qui créent des lésions sur l'ADN. La synthèse translésionnelle (TLS) permet à la cellule de répliquer l'ADN endommagé grâce à l'intervention d'ADN polymérases spécialisées. En réponse à des agents génotoxiques, le facteur de processivité PCNA, qui interagit avec les ADN polymérases réplicatives et translésionnelles, est mono-ubiquitiné par le complexe Rad6/Rad18. Durant ma thèse, j'ai cherché à (1) comprendre les évènements moléculaires qui déclenchent la mono-ubiquitination de PCNA et (2) à comprendre le rôle
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Dietsch, Frank. "Caractérisation des fonctions des modifications post-traductionnelles de PCNA à l'aide d'un nouvel outil génétique." Thesis, Strasbourg, 2019. http://www.theses.fr/2019STRAJ014/document.

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PCNA est une protéine essentielle qui intervient dans de nombreux mécanismes cellulaires et qui possède de nombreuses modifications post-traductionnelles (MPTs) dont les fonctions de certaines, restent encore inconnues. Afin d’étudier la fonction de ces MPTs, nous avons développé un nouvel outil génétique permettant in cellulo, de substituer la protéine endogène PCNA par une version mutée de la protéine appelée version de complémentation. La technique consiste à cotransfecter des cellules en culture avec deux types de plasmides. Un premier plasmide permet l’invalidation du gène de PCNA endogèn
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Fryzelková, Jana. "Úloha helikázy RECQ5 při stabilizaci a opravě replikačních vidlic po jejich kolizi s transkripčním komplexem." Master's thesis, 2017. http://www.nusl.cz/ntk/nusl-355971.

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The progression of replication forks can be slowed down or paused by various external and internal factors during DNA replication. This phenomenon is referred to as replication stress and substantially contributes to genomic instability that is a hallmark of cancer. Transcription complex belongs to the internal replication-interfering factors and represents a barrier for progression of the replication complex. The replication forks are slowed down or paused while passing through the transcriptionally active regions of the genome that can lead to subsequent collapse of stalled forks and formati
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