ArticleBMC molecular biology2004
Mapping and mutation of the conserved DNA polymerase interaction motif (DPIM) located in the C-terminal domain of fission yeast DNA polymerase delta subunit Cdc27.
Article in BMC molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Break-induced replication is enhanced by a phospho-activated RPA-binding module in Pol32.Nature communications · 2026Article
- How DNA secondary structures drive replication fork instability.DNA repair · 2025Review
- POLD3 as Controller of Replicative DNA Repair.International journal of molecular sciences · 2024Review
- DNA polymerase delta governs parental histone transfer to DNA replication lagging strand.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The processivity factor Pol32 mediates nuclear localization of DNA polymerase delta and prevents chromosomal fragile site formation in Drosophila development.PLoS genetics · 2019Article
- Loss of Pol32 in Drosophila melanogaster causes chromosome instability and suppresses variegation.PloS one · 2015Article
- Modulation of mutagenesis in eukaryotes by DNA replication fork dynamics and quality of nucleotide pools.Environmental and molecular mutagenesis · 2012Review
- Competition between replicative and translesion polymerases during homologous recombination repair in Drosophila.PLoS genetics · 2012Article
- DNA polymerases at the eukaryotic fork-20 years later.Mutation research · 2010Review
- Functional mapping of the fission yeast DNA polymerase delta B-subunit Cdc1 by site-directed and random pentapeptide insertion mutagenesis.BMC molecular biology · 2009Article
- X-ray structure of the complex of regulatory subunits of human DNA polymerase delta.Cell cycle (Georgetown, Tex.) · 2008Article
- Genetics of lagging strand DNA synthesis and maturation in fission yeast: suppression analysis links the Dna2-Cdc24 complex to DNA polymerase delta.Nucleic acids research · 2004Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundDNA polymerases alpha and delta play essential roles in the replication of chromosomal DNA in eukaryotic cells. DNA polymerase alpha (Pol alpha)-primase is required to prime synthesis of the leading strand and each Okazaki fragment on the lagging strand, whereas DNA polymerase delta (Pol delta) is required for the elongation stages of replication, a function it appears capable of performing on both leading and lagging strands, at least in the absence of DNA polymerase epsilon (Pol epsilon).
resultsHere it is shown that the catalytic subunit of Pol alpha, Pol1, interacts with Cdc27, one of three non-catalytic subunits of fission yeast Pol delta, both in vivo and in vitro. Pol1 interacts with the C-terminal domain of Cdc27, at a site distinct from the previously identified binding sites for Cdc1 and PCNA. Comparative protein sequence analysis identifies a protein sequence motif, called the DNA polymerase interaction motif (DPIM), in Cdc27 orthologues from a wide variety of eukaryotic species, including mammals. Mutational analysis shows that the DPIM in fission yeast Cdc27 is not required for effective DNA replication, repair or checkpoint function.
conclusionsA short protein sequence motif (DPIM) has been identified as mediating Pol alpha-Pol delta interactions in fission yeast. Despite being conserved across species, mutational analysis indicates the DPIM does not play an essential role in vivo, suggesting that interaction between the two polymerases is also non-essential.
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