ArticleNucleic acids research2008
Mechanistic consequences of temperature on DNA polymerization catalyzed by a Y-family DNA polymerase.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed.
- Substrate energetics in non-templated DNA synthesis by terminal deoxynucleotidyl transferase.Nucleic acids research · 2026Article
- Conformational gating governs nucleotide incorporation by a DNA-crosslinked polymerase.Nucleic acids research · 2026Article
- Biochemical and mutational studies of an endonuclease V from the hyperthermophilic crenarchaeon Sulfolobus islandicus REY15A.World journal of microbiology & biotechnology · 2023Article
- Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022Review
- Investigating the Conformational Dynamics of a Y-Family DNA Polymerase during Its Folding and Binding to DNA and a Nucleotide.JACS Au · 2022Article
- Kinetic investigation of the polymerase and exonuclease activities of human DNA polymerase ε holoenzyme.The Journal of biological chemistry · 2020Article
- Investigation of Intradomain Motions of a Y-Family DNA Polymerase during Substrate Binding and Catalysis.Biochemistry · 2016Article
- Single-Molecule Investigation of Response to Oxidative DNA Damage by a Y-Family DNA Polymerase.Biochemistry · 2016Article
- Dynamic conformational change regulates the protein-DNA recognition: an investigation on binding of a Y-family polymerase to its target DNA.PLoS computational biology · 2014Article
- Recent insight into the kinetic mechanisms and conformational dynamics of Y-Family DNA polymerases.Biochemistry · 2014Review
- Direct probing of solvent accessibility and mobility at the binding interface of polymerase (Dpo4)-DNA complex.The journal of physical chemistry. A · 2013Article
- Kinetic mechanism of DNA polymerization catalyzed by human DNA polymerase ε.Biochemistry · 2013Article
- Following DNA chain extension and protein conformational changes in crystals of a Y-family DNA polymerase via Raman crystallography.Biochemistry · 2013Article
- Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity.Biochemistry · 2012Article
- Quantitative analysis of the mutagenic potential of 1-aminopyrene-DNA adduct bypass catalyzed by Y-family DNA polymerases.Mutation research · 2012Article
- Identification of an unfolding intermediate for a DNA lesion bypass polymerase.Chemical research in toxicology · 2012Article
- Kinetics and fidelity of polymerization by DNA polymerase III from Sulfolobus solfataricus.Biochemistry · 2012Article
- Pre-Steady-State Kinetic Analysis of Truncated and Full-Length Saccharomyces cerevisiae DNA Polymerase Eta.Journal of nucleic acids · 2010Article
- Article
- Mechanistic studies of the bypass of a bulky single-base lesion catalyzed by a Y-family DNA polymerase.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Our previous publication shows that Sulfolobus solfataricus Dpo4 utilizes an 'induced-fit' mechanism to select correct incoming nucleotides at 37 degrees C. Here, we provide a comprehensive report elucidating the kinetic mechanism of a DNA polymerase at a reaction temperature higher than 37 degrees C in an attempt to determine the effect of temperature on enzyme fidelity and mechanism. The fidelity of Dpo4 did not change considerably with a 30 degrees C increase in reaction temperature, suggesting that the fidelity of Dpo4 at 80 degrees C is similar to that determined here at 56 degrees C. Amazingly, the incorporation rate for correct nucleotides increased by 18 900-fold from 2 degrees C to 56 degrees C, similar in magnitude to that observed for incorrect nucleotides, thus not perturbing fidelity. Three independent lines of kinetic evidence indicate that a protein conformational change limits correct nucleotide incorporations at 56 degrees C. Furthermore, the activation energy for the incorporation of a correct nucleotide was determined to be 32.9 kcal/mol, a value considerably larger than those values estimated for a rate-limiting chemistry step, providing a fourth line of evidence to further substantiate this conclusion. These results herein provide evidence that Dpo4 utilizes the 'induced-fit' mechanism to select a correct nucleotide at all temperatures.
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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.