Density- and elongation speed-dependent error correction in RNA polymerization [PDF]
, 2021 Backtracking of RNA polymerase (RNAP) is an important pausing mechanism during DNA transcription that is part of the error correction process that enhances transcription fidelity. We model the backtracking mechanism of RNA polymerase, which usually happens when the polymerase tries to incorporate a mismatched nucleotide triphosphate.
arxiv +1 more source
Engineered DNA Polymerase Improves PCR Results for Plastid DNA
Applications in Plant Sciences, 2013 Premise of the study: Secondary metabolites often inhibit PCR and sequencing reactions in extractions from plant material, especially from silica-dried and herbarium material.
Melanie Schori +3 more
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Accuracy and speed of elongation in a minimal model of DNA replication [PDF]
, 2021 Being a dual purpose enzyme, the DNA polymerase is responsible for elongation of the newly formed DNA strand as well as cleaving the erroneous growth in case of a misincorporation. The efficiency of replication depends on the coordination of the polymerization and exonuclease activity of DNA polymerase.
arxiv +1 more source
New link between the RNA polymerase II-CTD and replication stress
Molecular & Cellular Oncology, 2021 Conflicts between transcription and replication are a major source of replication stress. Our recent findings show that proper dephosphorylation of Serine 5 in the carboxy-terminal domain (CTD) of DNA-directed RNA polymerase II subunit RPB1 is needed to ...
Helga B. Landsverk +3 more
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Kinetics and thermodynamics of exonuclease-deficient DNA polymerases [PDF]
Phys. Rev. E 93, 042419 (2016), 2016 A kinetic theory is developed for exonuclease-deficient DNA polymerases, based on the experimental observation that the rates depend not only on the newly incorporated nucleotide, but also on the previous one, leading to the growth of Markovian DNA sequences from a Bernoullian template. The dependences on nucleotide concentrations and template sequence
arxiv +1 more source
Computational Investigations on Polymerase Actions in Gene Transcription and Replication Combining Physical Modeling and Atomistic Simulations [PDF]
Chin. Phys. B Vol. 25, No. 1 (2016) 018706, 2015 Polymerases are protein enzymes that move along nucleic acid chains and catalyze template-based polymerization reactions during gene transcription and replication. The polymerases also substantially improve transcription or replication fidelity through the non-equilibrium enzymatic cycles.
arxiv +1 more source
Mechanisms of PARP inhibitor resistance in cancer and insights into the DNA damage response
Genome Medicine, 2018 Editorial summary Inhibitors of poly(ADP-ribose) polymerase (PARPi) have entered the clinic for the treatment of patients with cancers that lack homology-directed DNA repair, but drug resistance remains a clinical hurdle.
Paola Francica, Sven Rottenberg
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The ability to form homodimers is essential for RDM1 to function in RNA-directed DNA methylation. [PDF]
PLoS ONE, 2014 RDM1 (RNA-DIRECTED DNA METHYLATION1) is a small plant-specific protein required for RNA-directed DNA methylation (RdDM). RDM1 interacts with RNA polymerase II (Pol II), ARGONAUTE4 (AGO4), and the de novo DNA methyltransferase DOMAINS REARRANGED ...
Taku Sasaki +4 more
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Kinetics and thermodynamics of DNA polymerases with exonuclease proofreading [PDF]
Phys. Rev. E 93, 042420 (2016), 2016 Kinetic theory and thermodynamics are applied to DNA polymerases with exonuclease activity, taking into account the dependence of the rates on the previously incorportated nucleotide. The replication fidelity is shown to increase significantly thanks to this dependence at the basis of the mechanism of exonuclease proofreading.
arxiv +1 more source
Amplification of 4–9-kb Human Genomic DNA Flanking a Known Site Using a Panhandle PCR Variant
BioTechniques, 1997 We present a method for the in vitro amplification of >6.0 kb of DNA flanking a known site. This is accomplished by ligating an oligonucleotide to create an inverted repeat of a portion of the known sequence, followed by single-primer polymerase chain ...
Douglas H. Jones, Stanley C. Winistorfer
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