Nucleotide Excision Repair Is Associated with the Replisome and Its Efficiency Depends on a Direct Interaction between XPA and PCNA
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Proliferating cell nuclear antigen (PCNA) is an essential protein for DNA replication, DNA repair, cell cycle regulation, chromatin remodeling, and epigenetics. Many proteins interact with PCNA through the PCNA interacting peptide (PIP)-box or the newly identified AlkB homolog 2 PCNA interacting motif (APIM). The xeroderma pigmentosum group A (XPA) protein, with a central but somewhat elusive role in nucleotide excision repair (NER), contains the APIM sequence suggesting an interaction with PCNA. With an in vivo based approach, using modern techniques in live human cells, we show that APIM in XPA is a functional PCNA interacting motif and that efficient NER of UV lesions is dependent on an intact APIM sequence in XPA. We show that XPA(-/-) cells complemented with XPA containing a mutated APIM sequence have increased UV sensitivity, reduced repair of cyclobutane pyrimidine dimers and (6-4) photoproducts, and are consequently more arrested in S phase as compared to XPA(-/-) cells complemented with wild type XPA. Notably, XPA colocalizes with PCNA in replication foci and is loaded on newly synthesized DNA in undamaged cells. In addition, the TFIIH subunit XPD, as well as XPF are loaded on DNA together with XPA, and XPC and XPG colocalize with PCNA in replication foci. Altogether, our results suggest a presence of the NER complex in the vicinity of the replisome and a novel role of NER in post-replicative repair.
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XPA may participate in other cellular events in the absence of genotoxic insults, such as facilitating chromatin modification for transcription, inhibiting DNA double-strand break repair in progeria, and potential involvement in DNA replication.
“In addition, recent studies demonstrated that besides its anticipated functions in NER, XPA also may participate in other cellular events in the absence of genotoxic insults, such as facilitating chromatin modification for transcription [27], inhibiting DNA double-strand break repair in progeria [28], and potential involvement in DNA replication [29].”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [29]
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- Authors
- Gilljam, K. M., Müller, R., Liabakk, N. B., & Otterlei, M.
- Affiliations
- Norwegian University of Science and Technology (NO)
- Corresponding author
- Otterlei, Marit
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-11-13
- Volume
- 7
- Issue
- 11
- Pages
- e49199
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3496702
- OpenAlex
- W2122374677
- Cited by
- 69
- References
- 48
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 4 · 2023: 1 · 2022: 5 · 2021: 3 · 2020: 6 · 2019: 3 · 2018: 6 · 2017: 11 · 2016: 5 · 2015: 6 · 2014: 10 · 2013: 4
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- BIBSYS Brage (BIBSYS (Norway)) (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- NORA - Norwegian Open Research Archives (submittedVersion, cc-by)
- Funders
- Kreftforeningen
- Norges Teknisk-Naturvitenskapelige Universitet
- Helse Midt-Norge
- Norges Forskningsråd
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- nucleotide excision repair, PCNA, XPA, UV-induced DNA damage, cyclobutane pyrimidine dimers, 6-4 photoproducts, S phase arrest, replisome, TFIIH, XPC, XPG, XPD, XPF
- MeSH terms
- Replisomes, Amino Acid Sequence, DNA-Directed DNA Polymerase, DNA Repair, DNA Replication, HeLa Cells, Histones, Humans, Models, Biological, Molecular Sequence Data, Multienzyme Complexes, Protein Binding, Structure-Activity Relationship, Ultraviolet Rays, Proliferating Cell Nuclear Antigen, Amino Acid Motifs, Protein Transport, Mutant Proteins, Xeroderma Pigmentosum Group A Protein, HEK293 Cells
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