ArticleNucleic acids research2015
FF483-484 motif of human Polη mediates its interaction with the POLD2 subunit of Polδ and contributes to DNA damage tolerance.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Homozygous substitution of threonine 191 by proline in polymerase η causes Xeroderma pigmentosum variant.Scientific reports · 2024Article
- DNA Damage Responses, the Trump Card of Stem Cells in the Survival Game.Advances in experimental medicine and biology · 2024Review
- Early embryonic lethality of mice lacking POLD2.Molecular reproduction and development · 2023Article
- POLD2 is activated by E2F1 to promote triple-negative breast cancer proliferation.Frontiers in oncology · 2022Article
- Genetic and physical interactions between Polη and Rev1 in response to UV-induced DNA damage in mammalian cells.Scientific reports · 2021Article
- Beyond the Lesion: Back to High Fidelity DNA Synthesis.Frontiers in molecular biosciences · 2021Review
- Yeast DNA polymerase η possesses two PIP-like motifs that bind PCNA and Rad6-Rad18 with different specificities.DNA repair · 2020Article
- ShRNA-based POLD2 expression knockdown sensitizes glioblastoma to DNA-Damaging therapeutics.Cancer letters · 2020Article
- Genome-wide Target Enrichment-aided Chip Design: a 66 K SNP Chip for Cashmere Goat.Scientific reports · 2017Article
- Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017Review
- Review
- Review
- Proteomic Profiling Reveals a Specific Role for Translesion DNA Polymerase η in the Alternative Lengthening of Telomeres.Cell reports · 2016Article
- R.I.P. to the PIP: PCNA-binding motif no longer considered specific: PIP motifs and other related sequences are not distinct entities and can bind multiple proteins involved in genome maintenance.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016Review
- Review
- Involvement of translesion synthesis DNA polymerases in DNA interstrand crosslink repair.DNA repair · 2016Review
- The Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1.The Journal of biological chemistry · 2016Article
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Switching between replicative and translesion synthesis (TLS) DNA polymerases are crucial events for the completion of genomic DNA synthesis when the replication machinery encounters lesions in the DNA template. In eukaryotes, the translesional DNA polymerase η (Polη) plays a central role for accurate bypass of cyclobutane pyrimidine dimers, the predominant DNA lesions induced by ultraviolet irradiation. Polη deficiency is responsible for a variant form of the Xeroderma pigmentosum (XPV) syndrome, characterized by a predisposition to skin cancer. Here, we show that the FF483-484 amino acids in the human Polη (designated F1 motif) are necessary for the interaction of this TLS polymerase with POLD2, the B subunit of the replicative DNA polymerase δ, both in vitro and in vivo. Mutating this motif impairs Polη function in the bypass of both an N-2-acetylaminofluorene adduct and a TT-CPD lesion in cellular extracts. By complementing XPV cells with different forms of Polη, we show that the F1 motif contributes to the progression of DNA synthesis and to the cell survival after UV irradiation. We propose that the integrity of the F1 motif of Polη, necessary for the Polη/POLD2 interaction, is required for the establishment of an efficient TLS complex.
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