Cited by 538DNA Repair MechanismsUbiquitin and proteasome pathwaysDNA and Nucleic Acid Chemistry

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Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination

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Watanabe, Kenji, Tateishi, Satoshi, Kawasuji, Michio, Tsurimoto, Toshiki, Inoue, Hirokazu, Yamaizumi, Masaru·2004·The EMBO Journal

DOI 10.1038/sj.emboj.7600383PMC PMC522788

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Abstract

The DNA replication machinery stalls at damaged sites on templates, but normally restarts by switching to a specialized DNA polymerase(s) that carries out translesion DNA synthesis (TLS). In human cells, DNA polymerase eta (poleta) accumulates at stalling sites as nuclear foci, and is involved in ultraviolet (UV)-induced TLS. Here we show that poleta does not form nuclear foci in RAD18(-/-) cells after UV irradiation. Both Rad18 and Rad6 are required for poleta focus formation. In wild-type cells, UV irradiation induces relocalization of Rad18 in the nucleus, thereby stimulating colocalization with proliferating cell nuclear antigen (PCNA), and Rad18/Rad6-dependent PCNA monoubiquitination. Purified Rad18 and Rad6B monoubiquitinate PCNA in vitro. Rad18 associates with poleta constitutively through domains on their C-terminal regions, and this complex accumulates at the foci after UV irradiation. Furthermore, poleta interacts preferentially with monoubiquitinated PCNA, but poldelta does not. These results suggest that Rad18 is crucial for recruitment of poleta to the damaged site through protein-protein interaction and PCNA monoubiquitination.

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Authors: Watanabe, K., Tateishi, S., Kawasuji, M., Tsurimoto, T., Inoue, H., & Yamaizumi, M.
Affiliations: Institute of Molecular Embryology and Genetics, Kumamoto University (JP)
Kumamoto University (JP)
Kyushu University (JP)
Saitama University (JP)
Corresponding author: Yamaizumi, Masaru
ORCID: Watanabe, Kenji
Tateishi, Satoshi
Tsurimoto, Toshiki
Inoue, Hirokazu
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2004-09-09
Volume: 23
Issue: 19
Pages: 3886-3896
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7600383
PMC: PMC522788
OpenAlex: W2020136215
Cited by: 538
References: 34
Citations by year: 2026: 5 · 2025: 15 · 2024: 22 · 2023: 15 · 2022: 16 · 2021: 18 · 2020: 18 · 2019: 14 · 2018: 27 · 2017: 18 · 2016: 24 · 2015: 21 · 2014: 19 · 2013: 23 · 2012: 37
FWCI: 11.96
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Princess Takamatsu Cancer Research Fund
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 › DNA and Nucleic Acid Chemistry
Keywords: RAD18, DNA polymerase eta, PCNA monoubiquitination, DNA replication stalling, translesion synthesis, UV-induced DNA damage, replication restart, protein-protein interaction, PCNA, DNA polymerase delta, nuclear foci, DNA damage response
MeSH terms: Y-Family DNA Polymerases, Animals, Cell Nucleus, DNA Polymerase III, DNA-Directed DNA Polymerase, DNA Replication, DNA-Binding Proteins, Female, Cricetinae, Humans, Male, Mice, Inbred C57BL, Ultraviolet Rays, CHO Cells, Proliferating Cell Nuclear Antigen, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Mice

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Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination

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