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Deoxyuridine triphosphatase

dUTPase, deoxyuridine triphosphatase, dUTP pyrophosphatase, DUT, dUTP nucleotidohydrolase, DUT1
This gene encodes an essential enzyme of nucleotide metabolism. The encoded protein forms a ubiquitous, homotetrameric enzyme that hydrolyzes dUTP to dUMP and pyrophosphate. This reaction serves two cellular purposes: providing a precursor (dUMP) for the synthesis of thymine nucleotides needed for DNA replication, and limiting intracellular pools of dUTP. Elevated levels of dUTP lead to increased incorporation of uracil into DNA, which induces extensive excision repair mediated by uracil glycosylase. This repair process, resulting in the removal and reincorporation of dUTP, is self-defeating and leads to DNA fragmentation and cell death. Alternative splicing of this gene leads to different isoforms that localize to either the mitochondrion or nucleus. A related pseudogene is located on chromosome 19. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, fibrillin-1, POLYMERASE
Papers on dUTPase
The Type 2 dUTPase of Bacteriophage ϕNM1 Initiates Mobilization of Staphylococcus aureus Bovine Pathogenicity Island 1.
Dokland et al., Birmingham, United States. In J Mol Biol, Dec 2015
One such SaPI, SaPIbov1, is derepressed by the dUTPase (Dut) of bacteriophage 80α (Dut80α) and its phage ϕ11 homolog, Dut11.
The 1,2-Diaminocyclohexane Carrier Ligand in Oxaliplatin Induces p53-Dependent Transcriptional Repression of Factors Involved in Thymidylate Biosynthesis.
Kitao et al., Fukuoka, Japan. In Mol Cancer Ther, Oct 2015
In the p53-proficient colorectal cancer cell line HCT116, oxaliplatin represses the expression of deoxyuridine triphosphatase (dUTPase), a ubiquitous pyrophosphatase that catalyzes the hydrolysis of dUTP to dUMP and inhibits dUTP-mediated cytotoxicity.
Identification and Characterization of Cyprinid Herpesvirus-3 (CyHV-3) Encoded MicroRNAs.
Walls et al., Galway, Ireland. In Plos One, 2014
We also present evidence that one confirmed miRNA can regulate the expression of a putative CyHV-3-encoded dUTPase.
dUTPase: the frequently overlooked enzyme encoded by many retroviruses.
Herzig et al., Tel Aviv-Yafo, Israel. In Retrovirology, 2014
Interestingly, a fourth virus-encoded enzyme, the deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) is also found in several major retroviral groups.
Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation.
Moriyama et al., Lincoln, United States. In Bmc Res Notes, 2014
BACKGROUND: Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) hydrolyzes dUTP to dUMP and pyrophosphate to maintain the cellular thymine-uracil ratio.
Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains.
Vertessy et al., Budapest, Hungary. In Plos One, 2014
Results suggest that a helix-turn-helix motif governs the interaction of the Stl protein with its cognate DNA site: point mutations within this motif drastically decrease DNA-binding ability, whereas the interaction with the Stl-binding partner protein dUTPase is unperturbed by these point mutations.
Novel developments in the use of antimetabolites.
Peters, Amsterdam, Netherlands. In Nucleosides Nucleotides Nucleic Acids, 2013
The cytidine-analog fluorocyclopentenylcytosine (RX-3117) is active in gemcitabine-resistant tumors and is activated by uridine-cytidine-kinase, can be incorporated into RNA and DNA and can downregulate DNA-methyltransferase-1. TAS-114 is a new generation dUTPase inhibitor.
Inhibition of dUTPase induces synthetic lethality with thymidylate synthase-targeted therapies in non-small cell lung cancer.
Ladner et al., Los Angeles, United States. In Mol Cancer Ther, 2012
Data sugget that inhibition of dUTPase is a mechanism-based therapeutic approach to significantly enhance the efficacy of thymidylate synthase (TS)-targeted chemotherapeutic agents.
Pharmacokinetic and metabolism determinants of fluoropyrimidines and oxaliplatin activity in treatment of colorectal patients.
Azzariti et al., Bari, Italy. In Curr Drug Metab, 2011
We analyzed predictive markers of fluoropyrimidines effectiveness, principally for 5-Fluorouracil (5- FU) and also for oral fluoropyrimidines, as thymidylate Synthase (TS), dihydropyrimidine dehydrogenase (DPD), orotate phosphoribosyl transferase (OPRT), methylenetetrahydrofolate reductase (MTHFR), deoxyuridine triphosphate nucleotidohydrolase (dUTPase), microsatellite instability.
Structure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme.
Yakunin et al., Toronto, Canada. In Biochem J, 2011
The structure of DUT1 and site-directed mutagenesis support a role of the conserved Phe142 in the interaction with the uracil base.
Cellular response to efficient dUTPase RNAi silencing in stable HeLa cell lines perturbs expression levels of genes involved in thymidylate metabolism.
Vértessy et al., Budapest, Hungary. In Nucleosides Nucleotides Nucleic Acids, 2011
Repression of dUTPase induced specific expression level increments for thymidylate kinase and thymidine kinase, and also an increased sensitization to 5-fluoro-2'-deoxyuridine and 5-fluoro-uracil.
Identification of potential pharmacogenomic markers of clinical efficacy of 5-fluorouracil in colorectal cancer.
Mini et al., Florence, Italy. In Int J Cancer, 2011
High dUTP pyrophosphatase is associated with recurrence in colorectal cancer patients undergoing 5-fluorouracil adjuvant chemotherapy
Drosophila proteins involved in metabolism of uracil-DNA possess different types of nuclear localization signals.
Vértessy et al., Budapest, Hungary. In Febs J, 2010
revealed the importance of the PAA(10-12) tripeptide and the ID(17-18) dipeptide, as well as the role of the PAAK(10-13) segment in nuclear localization of dUTPase.
DNA repair in Mycobacterium tuberculosis revisited.
Gicquel et al., Paris, France. In Fems Microbiol Rev, 2009
Novel characteristics of the M. tuberculosis DNA repair machinery have been found over the last decade, such as nonhomologous end joining, the presence of Mpg, ERCC3 and Hlr - proteins previously presumed to be produced exclusively in mammalian cells - and the recently discovered bifunctional dCTP deaminase:dUTPase.
Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases.
Tóth et al., Budapest, Hungary. In Acc Chem Res, 2009
To prevent uracil incorporation into DNA, representatives of the dUTP nucleotidohydrolase (dUTPase) enzyme family eliminate excess dUTP.
The contribution of DNA base damage to human cancer is modulated by the base excision repair interaction network.
Nilsen et al., Oslo, Norway. In Crit Rev Oncog, 2007
This review summarizes our current understanding of the contribution of DNA base damage to human cancer, with a particular focus on DNA-glycosylases and two of the main enzymes that prevent misincorporation of damaged deoxynucleotide triphosphates into DNA: the dUTPase and MTH1.
Herpes simplex virus DNA replication.
Lehman et al., Newark, United States. In Annu Rev Biochem, 1996
These enzymes include a deoxyuridine triphosphatase, a ribonucleotide reductase, a thymidine kinase, an alkaline endo-exonuclease, and a uracil-DNA glycosylase.
Crystal structure of a dUTPase.
Wilson et al., Stockholm, Sweden. In Nature, 1992
The enzyme dUTPase catalyses the hydrolysis of dUTP and maintains a low intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
The incorporation of uracil into animal cell DNA in vitro.
Goulian et al., In Cell, 1978
The high levels of dUTPase as well as the presence of RNA primers on most nascent DNA pieces (Tseng and Goulian, 1977) suggest that repair of uracil-containing DNA does not contribute to the generation of the small, nascent DNA pieces found during DNA synthesis in this in vitro system.
In vivo synthesis and properties of uracil-containing DNA.
Duncan et al., In Nature, 1978
T4 bacteriophage DNA containing as much as 30% of its thymine replaced by uracil can be synthesised in Escherichia coli deficient in both dUTPase and uracil--DNA glycosidase.
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