ArticleScientific reports2016
Trading in cooperativity for specificity to maintain uracil-free DNA.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- dUTPase is essential in zebrafish development and possesses several single-nucleotide variants with pronounced structural and functional consequences.FEBS open bio · 2026Article
- Full-length inhibitor protein is the most effective to perturb human dUTPase activity.Scientific reports · 2025Article
- Structural dynamics of human deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase).Scientific reports · 2024Article
- Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability.Scientific reports · 2021Article
- A user-friendly, high-throughput tool for the precise fluorescent quantification of deoxyribonucleoside triphosphates from biological samples.Nucleic acids research · 2020Article
- Beyond Chelation: EDTA Tightly Binds Taq DNA Polymerase, MutT and dUTPase and Directly Inhibits dNTPase Activity.Biomolecules · 2019Article
- Structural model of human dUTPase in complex with a novel proteinaceous inhibitor.Scientific reports · 2018Article
- Dissecting the link between the enzymatic activity and the SaPI inducing capacity of the phage 80α dUTPase.Scientific reports · 2017Article
- Differential control of dNTP biosynthesis and genome integrity maintenance by the dUTPase superfamily enzymes.Scientific reports · 2017Article
- Derepression of SaPIbov1 Is Independent of φNM1 Type 2 dUTPase Activity and Is Inhibited by dUTP and dUMP.Journal of molecular biology · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the dUTPase superfamily play an important role in the maintenance of the pyrimidine nucleotide balance and of genome integrity. dCTP deaminases and the bifunctional dCTP deaminase-dUTPases are cooperatively regulated by dTTP. However, the manifestation of allosteric behavior within the same trimeric protein architecture of dUTPases, the third member of the superfamily, has been a question of debate for decades. Therefore, we designed hybrid dUTPase trimers to access conformational states potentially mimicking the ones observed in the cooperative relatives. We studied how the interruption of different steps of the enzyme cycle affects the active site cross talk. We found that subunits work independently in dUTPase. The experimental results combined with a comparative structural analysis of dUTPase superfamily enzymes revealed that subtile structural differences within the allosteric loop and the central channel in these enzymes give rise to their dramatically different cooperative behavior. We demonstrate that the lack of allosteric regulation in dUTPase is related to the functional adaptation to more efficient dUTP hydrolysis which is advantageous in uracil-DNA prevention.
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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.