ArticleNucleic acids research2012
The C-terminus of Dpb2 is required for interaction with Pol2 and for cell viability.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- A thumb-domain insertion balances processivity and fidelity in DNA polymerase ε.Nucleic acids research · 2026Article
- Evidence for a functional interaction between yeast Pol ε and PCNA in vivo.Nucleic acids research · 2025Article
- The proofreading mechanism of the human leading-strand DNA polymerase ε holoenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Antagonistic interactions safeguard mitotic propagation of genetic and epigenetic information in zebrafish.Communications biology · 2024Article
- A sensor complements the steric gate when DNA polymerase ϵ discriminates ribonucleotides.Nucleic acids research · 2023Article
- Structure of the polymerase ε holoenzyme and atomic model of the leading strand replisome.Nature communications · 2020Article
- Sumoylation of the DNA polymerase ε by the Smc5/6 complex contributes to DNA replication.PLoS genetics · 2019Article
- Structural evidence for an essential Fe-S cluster in the catalytic core domain of DNA polymerase ϵ.Nucleic acids research · 2019Article
- Structure of DNA-CMG-Pol epsilon elucidates the roles of the non-catalytic polymerase modules in the eukaryotic replisome.Nature communications · 2018Article
- Diverse roles of Dpb2, the non-catalytic subunit of DNA polymerase ε.Current genetics · 2017Review
- Crystal structure of the human Polϵ B-subunit in complex with the C-terminal domain of the catalytic subunit.The Journal of biological chemistry · 2017Article
- CMG-Pol epsilon dynamics suggests a mechanism for the establishment of leading-strand synthesis in the eukaryotic replisome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Review
- Mutations in the Non-Catalytic Subunit Dpb2 of DNA Polymerase Epsilon Affect the Nrm1 Branch of the DNA Replication Checkpoint.PLoS genetics · 2017Article
- Human DNA polymerase ε is phosphorylated at serine-1940 after DNA damage and interacts with the iron-sulfur complex chaperones CIAO1 and MMS19.DNA repair · 2016Article
- Review
- Switching between polymerase and exonuclease sites in DNA polymerase ε.Nucleic acids research · 2015Article
- CMG helicase and DNA polymerase ε form a functional 15-subunit holoenzyme for eukaryotic leading-strand DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork.Nature structural & molecular biology · 2014Article
- Structural basis for processive DNA synthesis by yeast DNA polymerase ɛ.Nature structural & molecular biology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA polymerase ε (Pol ε) participates in the synthesis of the leading strand during DNA replication in Saccharomyces cerevisiae. Pol ε comprises four subunits: the catalytic subunit, Pol2, and three accessory subunits, Dpb2, Dpb3 and Dpb4. DPB2 is an essential gene with unclear function. A genetic screen was performed in S. cerevisiae to isolate lethal mutations in DPB2. The dpb2-200 allele carried two mutations within the last 13 codons of the open reading frame, one of which resulted in a six amino acid truncation. This truncated Dpb2 subunit was co-expressed with Pol2, Dpb3 and Dpb4 in S. cerevisiae, but this Dpb2 variant did not co-purify with the other Pol ε subunits. This resulted in the purification of a Pol2/Dpb3/Dpb4 complex that possessed high specific activity and high processivity and holoenzyme assays with PCNA, RFC and RPA on a single-primed circular template did not reveal any defects in replication efficiency. In conclusion, the lack of Dpb2 did not appear to have a negative effect on Pol ε activity. Thus, the C-terminal motif of Dpb2 that we have identified may instead be required for Dpb2 to fulfill an essential structural role at the replication origin or at the replication fork.
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