ArticleThe Journal of biological chemistry2008
Kinetic analysis of translesion synthesis opposite bulky N2- and O6-alkylguanine DNA adducts by human DNA polymerase REV1.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 70 citations in OpenAlex.
- The polymerase milieu of human papillomavirus.Journal of virology · 2026Review
- DamageFormer: a damage-aware multimodal deep learning framework for DNA lesion identification from nanopore sequencing.bioRxiv : the preprint server for biology · 2026Article
- Residues in the little finger domain of the Y-family Dpo4 DNA polymerase communicate to restrict synthesis past 8-oxoguanine lesions.Nucleic acids research · 2025Article
- Analysis of Novel DNA Adducts Derived from Acetaldehyde.Biomolecules · 2025Article
- Effects of the Y432S Cancer-Associated Variant on the Reaction Mechanism of Human DNA Polymerase κ.Journal of chemical information and modeling · 2024Article
- The Catalytic Activity of Human REV1 on Undamaged and Damaged DNA.International journal of molecular sciences · 2024Article
- Biochemical Activity of 17 Cancer-Associated Variants of DNA Polymerase Kappa Predicted by Electrostatic Properties.Chemical research in toxicology · 2023Article
- DNA Alkylation Damage by Nitrosamines and Relevant DNA Repair Pathways.International journal of molecular sciences · 2023Review
- Recent Advances in Understanding the Structures of Translesion Synthesis DNA Polymerases.Genes · 2022Review
- Probing altered enzyme activity in the biochemical characterization of cancer.Bioscience reports · 2022Review
- Making Choices: DNA Replication Fork Recovery Mechanisms.Seminars in cell & developmental biology · 2021Review
- Visualizing Rev1 catalyze protein-template DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Repair and translesion synthesis ofThe Journal of biological chemistry · 2019Article
- Quantification of DNA Lesions Induced by 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanol in Mammalian Cells.Chemical research in toxicology · 2019Article
- DNA replication studies ofThe Journal of biological chemistry · 2019Article
- Review
- Characterization of Nine Cancer-Associated Variants in Human DNA Polymerase κ.Chemical research in toxicology · 2018Article
- Structural Basis for the Interaction of Mutasome Assembly Factor REV1 with Ubiquitin.Journal of molecular biology · 2018Article
- Liquid Chromatography-Tandem Mass Spectrometry for the Quantification of Tobacco-Specific Nitrosamine-Induced DNA Adducts in Mammalian Cells.Analytical chemistry · 2017Article
- Kinetic and Structural Impact of Metal Ions and Genetic Variations on Human DNA Polymerase ι.The Journal of biological chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
REV1, a Y family DNA polymerase (pol), is involved in replicative bypass past DNA lesions, so-called translesion DNA synthesis. In addition to a structural role as a scaffold protein, REV1 has been proposed to play a catalytic role as a dCTP transferase in translesion DNA synthesis past abasic and guanine lesions in eukaryotes. To better understand the catalytic function of REV1 in guanine lesion bypass, purified recombinant human REV1 was studied with two series of guanine lesions, N(2)-alkylG adducts (in oligonucleotides) ranging in size from methyl (Me) to CH(2)(6-benzo[a]pyrenyl) (BP) and O(6)-alkylG adducts ranging from Me to 4-oxo-4-(3-pyridyl)butyl (Pob). REV1 readily produced 1-base incorporation opposite G and all G adducts except for O(6)-PobG, which caused almost complete blockage. Steady-state kinetic parameters (k(cat)/K(m)) were similar for insertion of dCTP opposite G and N(2)-G adducts but were severely reduced opposite the O(6)-G adducts. REV1 showed apparent pre-steady-state burst kinetics for dCTP incorporation only opposite N(2)-BPG and little, if any, opposite G, N(2)-benzyl (Bz)G, or O(6)-BzG. The maximal polymerization rate (k(pol) 0.9 s(-1)) opposite N(2)-BPG was almost the same as opposite G, with only slightly decreased binding affinity to dCTP (2.5-fold). REV1 bound N(2)-BPG-adducted DNA 3-fold more tightly than unmodified G-containing DNA. These results and the lack of an elemental effect ((S(p))-2'-deoxycytidine 5'-O-(1-thiotriphosphate)) suggest that the late steps after product formation (possibly product release) become rate-limiting in catalysis opposite N(2)-BPG. We conclude that human REV1, apparently the slowest Y family polymerase, is kinetically highly tolerant to N(2)-adduct at G but not to O(6)-adducts.
Indexed as
Identifiers
What OpenQuestion holds
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.