ArticleJournal of the American Chemical Society2011
A triad interaction in the fingers subdomain of DNA polymerase beta controls polymerase activity.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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.
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.
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Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- The S180R Human Germline Variant of DNA Polymerase β Is a Low Fidelity Enzyme with Reduced Flexibility of the Fingers Domain.Biochemistry · 2026Article
- SNP-Associated Substitutions of Amino Acid Residues in the dNTP Selection Subdomain Decrease Polβ Polymerase Activity.Biomolecules · 2024Article
- Intrinsic Peroxidase-like Activity of Ficin.Scientific reports · 2017Article
- Structural Insights into the Post-Chemistry Steps of Nucleotide Incorporation Catalyzed by a DNA Polymerase.Journal of the American Chemical Society · 2017Article
- Estrogen Drives Cellular Transformation and Mutagenesis in Cells Expressing the Breast Cancer-Associated R438W DNA Polymerase Lambda Protein.Molecular cancer research : MCR · 2016Article
- Induced Fit in the Selection of Correct versus Incorrect Nucleotides by DNA Polymerase β.Biochemistry · 2016Article
- Fluorescence resonance energy transfer studies of DNA polymerase β: the critical role of fingers domain movements and a novel non-covalent step during nucleotide selection.The Journal of biological chemistry · 2014Article
- The S229L colon tumor-associated variant of DNA polymerase β induces cellular transformation as a result of decreased polymerization efficiency.The Journal of biological chemistry · 2014Article
- Metal-dependent conformational activation explains highly promutagenic replication across O6-methylguanine by human DNA polymerase β.Journal of the American Chemical Society · 2014Article
- Sequence context modulation of polycyclic aromatic hydrocarbon-induced mutagenesis.Environmental and molecular mutagenesis · 2013Article
- Catalytic effects of mutations of distant protein residues in human DNA polymerase β: theory and experiment.Biochemistry · 2012Article
- Human POLB gene is mutated in high percentage of colorectal tumors.The Journal of biological chemistry · 2012Article
- Colon cancer-associated DNA polymerase β variant induces genomic instability and cellular transformation.The Journal of biological chemistry · 2012Article
- The E288K colon tumor variant of DNA polymerase β is a sequence specific mutator.Biochemistry · 2012Article
- Unfavorable electrostatic and steric interactions in DNA polymerase β E295K mutant interfere with the enzyme's pathway.Journal of the American Chemical Society · 2012Article
- The human gastric cancer-associated DNA polymerase β variant D160N is a mutator that induces cellular transformation.DNA repair · 2012Article
- A germline polymorphism of DNA polymerase beta induces genomic instability and cellular transformation.PLoS genetics · 2012Article
- Nucleosome disruption by DNA ligase III-XRCC1 promotes efficient base excision repair.Molecular and cellular biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
DNA polymerase beta (pol beta) is the main polymerase involved in the base excision repair pathway responsible for repairing damaged bases in the DNA. Previous studies on the H285D mutant of pol beta suggested that the C-terminal region of the polymerase is important for polymerase function. In this study, the C-terminal region of pol beta was mutated to assess its role in polymerization. Kinetic experiments showed that the C-terminal region is required for wild-type polymerase activity. Additionally, an interaction between the fingers and palm subdomain revealed itself to be required for polymerase activity. The E316R mutant of pol beta was shown to have a 29,000-fold reduction in polymerization rate with no reduction in nucleotide binding, suggesting that there exists a noncovalent mechanistic step between nucleotide binding and nucleophilic attack of the primer 3'-hydroxyl group on the α-PO(4) of the nucleotide. Molecular modeling studies of the E316R mutant demonstrate that disrupting the interaction between Arg182 and Glu316 disrupts the packing of side chains in the hydrophobic hinge region and may be hampering the conformational change during polymerization. Taken together, these data demonstrate that the triad interaction of Arg182, Glu316, and Arg333 is crucial for polymerase function.
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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.