Cited by 259DNA Repair MechanismsUbiquitin and proteasome pathwaysGenomics and Chromatin Dynamics

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Ubiquitin-dependent DNA damage bypass is separable from genome replication

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Daigaku, Yasukazu, Davies, Adelina A., Ulrich, Helle D.·2010·Nature

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Abstract

Post-replication repair (PRR) is a pathway that allows cells to bypass or overcome lesions during DNA replication. In eukaryotes, damage bypass is activated by ubiquitylation of the replication clamp PCNA through components of the RAD6 pathway. Whereas monoubiquitylation of PCNA allows mutagenic translesion synthesis by damage-tolerant DNA polymerases, polyubiquitylation is required for an error-free pathway that probably involves a template switch to the undamaged sister chromatid. Both the timing of PRR events during the cell cycle and their location relative to replication forks, as well as the factors required downstream of PCNA ubiquitylation, have remained poorly characterized. Here we demonstrate that the RAD6 pathway normally operates during S phase. However, using an inducible system of DNA damage bypass in budding yeast (Saccharomyces cerevisiae), we show that the process is separable in time and space from genome replication, thus allowing direct visualization and quantification of productive PRR tracts. We found that both during and after S phase ultraviolet-radiation-induced lesions are bypassed predominantly via translesion synthesis, whereas the error-free pathway functions as a backup system. Our approach has revealed the distribution of PRR tracts in a synchronized cell population. It will allow an in-depth mechanistic analysis of how cells manage the processing of lesions to their genomes during and after replication.

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Janke, C., Magiera, M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno-Borchart, A. C., Doenges, G., Schwob, E., Schiebel, E., et al. (2004) · Yeast · doi:10.1002/yea.1142 · Cited by 2,251
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202
EUKARYOTIC TRANSLESION SYNTHESIS DNA POLYMERASES: Specificity of Structure and Function
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Replicon Clusters Are Stable Units of Chromosome Structure: Evidence That Nuclear Organization Contributes to the Efficient Activation and Propagation of S Phase in Human Cells
Jackson, D., & Pombo, A. (1998) · Journal of Cell Biology · doi:10.1083/jcb.140.6.1285 · Cited by 881
Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
Stelter, P., & Ulrich, H. D. (2003) · Nature · doi:10.1038/nature01965 · Cited by 850
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Kannouche, P. L., Wing, J., & Lehmann, A. R. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00259-x · Cited by 845
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Johnson, R. E., Washington, M. T., Haracska, L., Prakash, S., & Prakash, L. (2000) · Nature · doi:10.1038/35023030 · Cited by 632
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Lopes, M., Foiani, M., & Sogo, J. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.11.015 · Cited by 563
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Watanabe, K., Tateishi, S., Kawasuji, M., Tsurimoto, T., Inoue, H., & Yamaizumi, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600383 · Cited by 538
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Authors: Daigaku, Y., Davies, A. A., & Ulrich, H. D.
Affiliations: Cancer Research UK (GB)
Corresponding author: Ulrich, Helle D.
ORCID: Daigaku, Yasukazu
Ulrich, Helle D.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2010-05-09
Volume: 465
Issue: 7300
Pages: 951-955
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature09097
PMC: PMC2888004
OpenAlex: W2080574942
Cited by: 259
References: 30
Citations by year: 2026: 8 · 2025: 8 · 2024: 9 · 2023: 4 · 2022: 6 · 2021: 15 · 2020: 15 · 2019: 13 · 2018: 21 · 2017: 16 · 2016: 26 · 2015: 15 · 2014: 18 · 2013: 22 · 2012: 27
FWCI: 11.08
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: Cancer Research UK (A7123, A10152)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: DNA damage bypass, translesion synthesis, error-free bypass, genome replication, S phase, Saccharomyces cerevisiae, replication fork, DNA polymerase, monoubiquitylation, polyubiquitination, template switching, sister chromatids, cell cycle synchronization
MeSH terms: Cell Cycle, Chromatin, DNA Damage, DNA Replication, Saccharomyces cerevisiae, Time Factors, Ultraviolet Rays, Genome, Proliferating Cell Nuclear Antigen, Ubiquitin, Saccharomyces cerevisiae Proteins, Ubiquitin-Conjugating Enzymes

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Ubiquitin-dependent DNA damage bypass is separable from genome replication

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