ArticleMolecular and cellular biology2005
A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesis.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 60 citations in OpenAlex.
- Translesion DNA synthesis on pyrimidine dimers by plant organellar DNA polymerases is metal-dependent.Nucleic acids research · 2026Article
- REV1 coordinates a multi-faceted tolerance response to DNA alkylation damage and prevents chromosome shattering in Drosophila melanogaster.PLoS genetics · 2024Article
- Protein Assemblies in Translesion Synthesis.Genes · 2024Review
- E3 ubiquitin ligase RNF2 protects polymerase ι from destabilization.Biochimica et biophysica acta. Molecular cell research · 2024Article
- Analysis of translesion polymerases in colorectal cancer cells following cetuximab treatment: A network perspective.Cancer medicine · 2024Article
- A Novel Interaction Between RAD23A/B and Y-family DNA Polymerases.Journal of molecular biology · 2023Article
- Polymerase iota (Pol ι) prevents PrimPol-mediated nascent DNA synthesis and chromosome instability.Science advances · 2023Article
- The ubiquitin-binding domain of DNA polymerase η directly binds to DNA clamp PCNA and regulates translesion DNA synthesis.The Journal of biological chemistry · 2022Article
- DNA polymerase ι compensates for Fanconi anemia pathway deficiency by countering DNA replication stress.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Quaternary structural diversity in eukaryotic DNA polymerases: monomeric to multimeric form.Current genetics · 2020Review
- Identification of PCNA-interacting protein motifs in human DNA polymerase δ.Bioscience reports · 2020Article
- Human DNA polymerase delta is a pentameric holoenzyme with a dimeric p12 subunit.Life science alliance · 2019Article
- A novel non-canonical PIP-box mediates PARG interaction with PCNA.Nucleic acids research · 2017Article
- Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017Review
- The herpes simplex virus 1 UL36USP deubiquitinase suppresses DNA repair in host cells via deubiquitination of proliferating cell nuclear antigen.The Journal of biological chemistry · 2017Article
- Monoubiquitylation of histone H2B contributes to the bypass of DNA damage during and after DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Posttranslational Regulation of Human DNA Polymerase ι.The Journal of biological chemistry · 2015Article
- Different types of interaction between PCNA and PIP boxes contribute to distinct cellular functions of Y-family DNA polymerases.Nucleic acids research · 2015Article
- Identification of two functional PCNA-binding domains in human DNA polymerase κ.Genes to cells : devoted to molecular & cellular mechanisms · 2014Article
- A novel mechanism for regulating the activity of proliferating cell nuclear antigen by a small protein.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
DNA polymerases (Pols) of the Y family rescue stalled replication forks by promoting replication through DNA lesions. Humans have four Y family Pols, eta, iota, kappa, and Rev1, of which Pols eta, iota, and kappa have been shown to physically interact with proliferating cell nuclear antigen (PCNA) and be functionally stimulated by it. However, in sharp contrast to the large increase in processivity that PCNA binding imparts to the replicative Pol, Poldelta, the processivity of Y family Pols is not enhanced upon PCNA binding. Instead, PCNA binding improves the efficiency of nucleotide incorporation via a reduction in the apparent K(m) for the nucleotide. Here we show that Poliota interacts with PCNA via only one of its conserved PCNA binding motifs, regardless of whether PCNA is bound to DNA or not. The mode of PCNA binding by Poliota is quite unlike that in Poldelta, where multisite interactions with PCNA provide for a very tight binding of the replicating Pol with PCNA. We discuss the implications of these observations for the accuracy of DNA synthesis during translesion synthesis and for the process of Pol exchange at the lesion site.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.