ArticleNucleic acids research2008
The solution structure of the amino-terminal domain of human DNA polymerase epsilon subunit B is homologous to C-domains of AAA+ proteins.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- Site directed mutagenesis reveals functional importance of conserved amino acid residues within the N-terminal domain of Dpb2 in budding yeast.Archives of microbiology · 2024Article
- Synergism between CMG helicase and leading strand DNA polymerase at replication fork.Nature communications · 2023Article
- Structure of a human replisome shows the organisation and interactions of a DNA replication machine.The EMBO journal · 2021Article
- Kinetic investigation of the polymerase and exonuclease activities of human DNA polymerase ε holoenzyme.The Journal of biological chemistry · 2020Article
- Structure of the polymerase ε holoenzyme and atomic model of the leading strand replisome.Nature communications · 2020Article
- Structure of DNA-CMG-Pol epsilon elucidates the roles of the non-catalytic polymerase modules in the eukaryotic replisome.Nature communications · 2018Article
- 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
- Crystal Structure of the Human Pol α B Subunit in Complex with the C-terminal Domain of the Catalytic Subunit.The Journal of biological chemistry · 2015Article
- Structural basis for processive DNA synthesis by yeast DNA polymerase ɛ.Nature structural & molecular biology · 2014Article
- DNA replication and homologous recombination factors: acting together to maintain genome stability.Chromosoma · 2013Review
- Domain structures and inter-domain interactions defining the holoenzyme architecture of archaeal d-family DNA polymerase.Life (Basel, Switzerland) · 2013Review
- Modulation of mutagenesis in eukaryotes by DNA replication fork dynamics and quality of nucleotide pools.Environmental and molecular mutagenesis · 2012Review
- The C-terminus of Dpb2 is required for interaction with Pol2 and for cell viability.Nucleic acids research · 2012Article
- Structure of a DNA polymerase alpha-primase domain that docks on the SV40 helicase and activates the viral primosome.The Journal of biological chemistry · 2010Article
- Defective interaction between Pol2p and Dpb2p, subunits of DNA polymerase epsilon, contributes to a mutator phenotype in Saccharomyces cerevisiae.Mutation research · 2009Article
- Functional mapping of the fission yeast DNA polymerase delta B-subunit Cdc1 by site-directed and random pentapeptide insertion mutagenesis.BMC molecular biology · 2009Article
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
DNA polymerases alpha, delta and epsilon are large multisubunit complexes that replicate the bulk of the DNA in the eukaryotic cell. In addition to the homologous catalytic subunits, these enzymes possess structurally related B subunits, characterized by a carboxyterminal calcineurin-like and an aminoproximal oligonucleotide/oligosaccharide binding-fold domain. The B subunits also share homology with the exonuclease subunit of archaeal DNA polymerases D. Here, we describe a novel domain specific to the N-terminus of the B subunit of eukaryotic DNA polymerases epsilon. The N-terminal domain of human DNA polymerases epsilon (Dpoe2NT) expressed in Escherichia coli was characterized. Circular dichroism studies demonstrated that Dpoe2NT forms a stable, predominantly alpha-helical structure. The solution structure of Dpoe2NT revealed a domain that consists of a left-handed superhelical bundle. Four helices are arranged in two hairpins and the connecting loops contain short beta-strand segments that form a short parallel sheet. DALI searches demonstrated a striking structural similarity of the Dpoe2NT with the alpha-helical subdomains of ATPase associated with various cellular activity (AAA+) proteins (the C-domain). Like C-domains, Dpoe2NT is rich in charged amino acids. The biased distribution of the charged residues is reflected by a polarization and a considerable dipole moment across the Dpoe2NT. Dpoe2NT represents the first C-domain fold not associated with an AAA+ protein.
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