ArticleProceedings of the National Academy of Sciences of the United States of America2013
DNA polymerase δ-interacting protein 2 is a processivity factor for DNA polymerase λ during 8-oxo-7,8-dihydroguanine bypass.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Knockout of AMD-associated geneAging · 2023Article
- Translesion DNA synthesis mediates acquired resistance to olaparib plus temozolomide in small cell lung cancer.Science advances · 2022Article
- The polymerase δ-interacting protein family and their emerging roles in diseases.Frontiers in medicine · 2022Review
- Crystal structure and molecular dynamics of human POLDIP2, a multifaceted adaptor protein in metabolism and genome stability.Protein science : a publication of the Protein Society · 2021Article
- A unique arginine cluster in PolDIP2 enhances nucleotide binding and DNA synthesis by PrimPol.Nucleic acids research · 2021Article
- Article
- Mechanisms for Maintaining Eukaryotic Replisome Progression in the Presence of DNA Damage.Frontiers in molecular biosciences · 2021Review
- Polymerase-δ-interacting protein 2 activates the RhoGEF epithelial cell transforming sequence 2 in vascular smooth muscle cells.American journal of physiology. Cell physiology · 2019Article
- Article
- Phosphorylation Alters the Properties of Pol η: Implications for Translesion Synthesis.iScience · 2018Article
- Gene expression changes associated with chemotherapy resistance in Ewing sarcoma cells.Molecular and clinical oncology · 2018Article
- Polymerase delta-interacting protein 2 deficiency protects against blood-brain barrier permeability in the ischemic brain.Journal of neuroinflammation · 2018Article
- Impaired oxidative stress response characterizes HUWE1-promoted X-linked intellectual disability.Scientific reports · 2017Article
- Review
- DNA Damage Tolerance by Eukaryotic DNA Polymerase and Primase PrimPol.International journal of molecular sciences · 2017Review
- Polymerase δ-interacting Protein 2: A Multifunctional Protein.Journal of cardiovascular pharmacology · 2017Review
- Ribonucleotide incorporation by human DNA polymerase η impacts translesion synthesis and RNase H2 activity.Nucleic acids research · 2017Article
- Translesion Synthesis of 2'-Deoxyguanosine Lesions by Eukaryotic DNA Polymerases.Chemical research in toxicology · 2017Article
- PrimPol-Prime Time to Reprime.Genes · 2017Review
- DNA polymerases in the mitochondria: A critical review of the evidence.Frontiers in bioscience (Landmark edition) · 2017Review
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Authors and funding
8 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bypass of DNA lesions by the replication fork requires a switch between the replicative DNA polymerase (Pol) and a more specialized translesion synthesis (TLS) Pol to overcome the obstacle. DNA Pol δ-interacting protein 2 (PolDIP2) has been found to physically interact with Pol η, Pol ζ, and Rev1, suggesting a possible role of PolDIP2 in the TLS reaction. However, the consequences of PolDIP2 interaction on the properties of TLS Pols remain unknown. Here, we analyzed the effects of PolDIP2 on normal and TLS by five different human specialized Pols from three families: Pol δ (family B), Pol η and Pol ι (family Y), and Pol λ and Pol β (family X). Our results show that PolDIP2 also physically interacts with Pol λ, which is involved in the correct bypass of 8-oxo-7,8-dihydroguanine (8-oxo-G) lesions. This interaction increases both the processivity and catalytic efficiency of the error-free bypass of a 8-oxo-G lesion by both Pols η and λ, but not by Pols β or ι. Additionally, we provide evidence that PolDIP2 stimulates Pol δ without affecting its fidelity, facilitating the switch from Pol δ to Pol λ during 8-oxo-G TLS. PolDIP2 stimulates Pols λ and η mediated bypass of other common DNA lesions, such as abasic sites and cyclobutane thymine dimers. Finally, PolDIP2 silencing increases cell sensitivity to oxidative stress and its effect is further potentiated in a Pol λ deficient background, suggesting that PolDIP2 is an important mediator for TLS.
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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.