Search results for "Nucleotidyltransferases"

showing 10 items of 22 documents

Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man

2015

AbstractThe ubiquitin-like protein Urm1 from budding yeast and its E1-like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways. To study whether these are conserved among eukaryotes, we used gene shuffles to replace the yeast proteins by their human counterparts, hURM1 and hUBA4/MOCS3. As judged from biochemical and genetical assays, hURM1 and hUBA4 are functional in yeast, albeit at reduced efficiencies. They mediate urmylation of the peroxiredoxin Ahp1, a known urmylation target in yeast, and support tRNA thiolation. Similar to hUBA4, yeast Uba4 itself is modified by Urm1 and hURM1 suggesting target overlap between eukaryal urmylation pathways. In sum, our st…

Saccharomyces cerevisiae ProteinsUba4 (hUBA4/MOCS3)Saccharomyces cerevisiaeBiophysicstRNA thiolationSaccharomyces cerevisiaeBiochemistryUbiquitin-like urmylationRNA TransferUbiquitinStructural BiologyAnticodonGeneticsHumansUbiquitinsMolecular BiologyProtein urmylationGeneUrm1 (hURM1)Conserved SequenceSequence Homology Amino AcidbiologyActivator (genetics)TRNA thiolationCell Biologybiology.organism_classificationNucleotidyltransferasesYeastBiochemistrySulfurtransferasesbiology.proteinPeroxiredoxinHeLa CellsFEBS Letters
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Spatial analysis of plant metabolism: Sucrose imaging within Vicia faba cotyledons reveals specific developmental patterns

2002

During legume embryogenesis the differentiation of the cotyledons proceeds gradually in a wave-like manner. The process is metabolically and genetically controlled and regulated by sugars. In order to perform a spatial and temporal analysis of the sugar distribution pattern a new method was developed to specifically measure sucrose directly in tissues via bioluminescence and single photon counting. This enabled a quantitative sucrose imaging with a resolution close to the single cell level. The procedure was applied on sections of Vicia faba cotyledons covering the main stages of histodifferentiation. Young embryos before the storage phase contained moderate levels of sucrose, which were ev…

SucroseSucrosefood.ingredientLightStarchGlucose-1-Phosphate AdenylyltransferasePlant ScienceBiologyCarbohydrate metabolismPlant Epidermischemistry.chemical_compoundfoodGeneticsSugarCell SizePlant ProteinsMembrane Transport Proteinsfood and beveragesCell DifferentiationFabaceaeStarchCell BiologyCarbohydrateNucleotidyltransferasesVicia fabachemistryBiochemistryGlucosyltransferasesLuminescent MeasurementsSeedsbiology.proteinCarbohydrate MetabolismSucrose synthaseCotyledonSignal TransductionThe Plant Journal
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Differential mode of inhibition of terminal deoxynucleotidyl transferase by 3′-dATP, ATP, βaraATP and αaraATP

1978

TUNEL assayArabinonucleotidesChemistryBiophysicsThymus GlandCell BiologyBiochemistryMolecular biologyStructure-Activity RelationshipAdenosine TriphosphateDeoxyadenine NucleotidesTerminal deoxynucleotidyl transferaseDNA NucleotidylexotransferaseStructural BiologyDNA NucleotidyltransferasesGeneticsAnimalsCattleMolecular BiologyDifferential (mathematics)FEBS Letters
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Alterations of Activities of Ribonucleases and Polyadenylate Polymerase in Synchronized Mouse L Cells

1977

The activities of the three known catabolic and the one anabolic polyadenylate enzymes have been determined in synchronized L5178y cells: endoribonuclease, exoribonuclease, 5'-nucleotidase and poly(A) polymerase (Mg2+-dependent). These four enzymes were found primarily in the nuclear fraction. The activity of poly(A) polymerase remains essentially constant during the transition from G1 to S phase. However, the poly(A) catabolic enzyme activities increase parallel with DNA synthesis; the endoribonuclease activity increases 4-fold during G1 to S phase, the exoribonuclease and the nucleotidase activities increasing 30-fold and 16-fold. During the S phase the poly(A)-degrading enzymes are far m…

Time FactorsEndoribonuclease activityEndoribonucleaseMitosisBiochemistryCell LineStructure-Activity RelationshipL CellsRibonucleasesExoribonucleaseNucleotidasePolyadenylatePolymerasechemistry.chemical_classificationbiologyDNA synthesisPolynucleotide AdenylyltransferaseNucleotidyltransferasesMolecular biologyMolecular WeightKineticsEnzymeBiochemistrychemistrybiology.proteinCell DivisionEuropean Journal of Biochemistry
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P sequences ofDrosophilla Subobscuralack exon 3 and may encode a 66 kd repressor-like protein

1991

Abstract Several P homologous sequences have been cloned and sequenced from Drosophila subobscura. These sequences are located at the 85DE region of the O chromosome and at least three of them are organized in tandem. We have identified four copies which exhibit strong similarity between them. All of the isolated elements are truncated at the 5' and 3' ends. They have lost the inverted terminal repeats and exon 3, but maintain exons 0, 1 and 2. They are transcribed producing a polyadenylated RNA. The structure of these transcripts suggests that they are able to encode a 66 kd repressor-like protein, but not a functional transposase. We ask about the biological role of a potential repressor …

Transposable elementMolecular Sequence DataRestriction MappingTransposasesRepressorBiologyHomology (biology)P elementExonSequence Homology Nucleic AcidGeneticsAnimalsAmino Acid SequenceCloning MolecularTransposaseRepetitive Sequences Nucleic AcidGeneticsLeucine ZippersBase SequenceNucleic acid sequenceNucleic Acid HybridizationExonsNucleotidyltransferasesMolecular biologyDrosophila subobscuraRepressor ProteinsDNA Transposable ElementsDrosophilaNucleic Acids Research
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RNA dependent DNA polymerase in cells of xeroderma pigmentosum

1971

Abstract Cells from X.P. ∗ skin contain an RNA dependent DNA polymerase, while in cells from normal skin this enzyme is lacking. This finding stimulates the thought that carcinogenesis in X.P. cells is due to an infection with an oncogenic RNA virus.

Xeroderma pigmentosumHepatitis B virus DNA polymeraseDNA polymeraseDNA polymerase IIDeoxyribonucleotidesPolynucleotidesBiophysicsRNA-dependent RNA polymeraseTritiummedicine.disease_causeRauscher VirusBiochemistryMicemedicineAnimalsChemical PrecipitationHumansMolecular BiologySkinchemistry.chemical_classificationXeroderma Pigmentosumintegumentary systembiologyRNA virusDNATemplates GeneticCell BiologyRibonucleotidesmedicine.diseasebiology.organism_classificationVirologyMolecular biologyStimulation ChemicalEnzymechemistryAmmonium SulfateDNA Nucleotidyltransferasesbiology.proteinRNAFemaleGuanosine TriphosphateCarcinogenesisBiochemical and Biophysical Research Communications
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Bleomycin, a selective inhibitor of DNA-dependent DNA polymerase from oncogenic RNA viruses.

1972

Abstract Bleomycin, an antibiotic, inhibits the DNA-dependent DNA polymerase from Rauscher murine leukemia virus. Higher concentrations of BLM ∗ are required to inhibit it's RNA-dependent DNA polymerase. These inhibition effects of the non-competitive type are not altered by preincubation of the DNA with BLM. Under comparable conditions neither the DNA-dependent DNA polymerase activity from E. coli and mouse liver nor the DNA-dependent RNA polymerase activity from mouse lymphoma cells are affected by BLM.

congenital hereditary and neonatal diseases and abnormalitiesTime FactorsLymphomaDNA polymeraseHepatitis B virus DNA polymeraseUracil NucleotidesDNA polymerase IIBiophysicsRNA-dependent RNA polymeraseCytosine NucleotidesTritiumBiochemistryRauscher VirusCell LineBleomycinMiceEscherichia coliAnimalsMolecular BiologyPolymeraseDNA clampAntibiotics Antineoplasticbiologyurogenital systemnutritional and metabolic diseasesCell BiologyDNAMolecular biologyReverse transcriptaseKineticsReal-time polymerase chain reactionLiverDNA Nucleotidyltransferasesbiology.proteinRNABiochemical and biophysical research communications
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Activity and kinetics of DNA dependent DNA and RNA polymerases n xeroderma pigmentosum and in normal human skin.

1971

1. DNA dependent DNA polymerase (E.C.2.7.7.7) was prepared from human normal and from Xeroderma pigmentosum skin. 2. DNA polymerase from normal skin has the same Michaelis constant with native and denatured DNA as templateKm= 120 ± 11 µg DNA/ml, with differing maximum reaction velocities. 3. The enzyme from Xeroderma pigmentosum has the same Michaelis constant for denatured DNA as the enzyme from normal skin, but with native DNA as template, theKmvalue is lower (97.2 ± 9.8). The maximum reaction velocities of the Xeroderma pigmentosum enzyme with native resp. denatured DNA as template are the same. 4. DNA dependent RNA polymerases (E.C.2.7.7.6) from normal and Xeroderma pigmentosum skin wer…

congenital hereditary and neonatal diseases and abnormalitiesXeroderma pigmentosumDNA polymeraseDNA polymerase IIDermatologyTritiumEndonucleasechemistry.chemical_compoundmedicineHumansskin and connective tissue diseasesPolymeraseSkinCarbon IsotopesXeroderma PigmentosumDNA clampintegumentary systembiologynutritional and metabolic diseasesRNA NucleotidyltransferasesGeneral MedicineDNAClinical Enzyme Testsmedicine.diseaseMolecular biologyEnzyme ActivationchemistryDNA Nucleotidyltransferasesbiology.proteinPrimer (molecular biology)DNAArchiv fur dermatologische Forschung
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Analysis of the Cellular Roles of MOCS3 Identifies a MOCS3-Independent Localization of NFS1 at the Tips of the Centrosome

2019

The deficiency of the molybdenum cofactor (Moco) is an autosomal recessive disease, which leads to the loss of activity of all molybdoenzymes in humans with sulfite oxidase being the essential protein. Moco deficiency generally results in death in early childhood. Moco is a sulfur-containing cofactor synthesized in the cytosol with the sulfur being provided by a sulfur relay system composed of the L-cysteine desulfurase NFS1, MOCS3, and MOCS2A. Human MOCS3 is a dual-function protein that was shown to play an important role in Moco biosynthesis and in the mcm(5)s(2) U thio modifications of nucleosides in cytosolic tRNAs for Lys, Gln, and Glu. In this study, we constructed a homozygous MOCS3 …

inorganic chemicalsCoenzymesBiochemistry03 medical and health scienceschemistry.chemical_compoundRNA Transferddc:570Sulfite oxidaseMetalloproteinsHumansnatural sciencesInstitut für Biochemie und BiologieAconitate HydrataseCentrosome0303 health sciencesPteridinesSulfite Oxidase030302 biochemistry & molecular biologyNucleotidyltransferasesIsocitrate DehydrogenaseCell biologyCarbon-Sulfur LyasesHEK293 CellschemistryCentrosomeSulfurtransferasesbacteriaCRISPR-Cas SystemsMolybdenum cofactorMolybdenum CofactorsHeLa CellsBiochemistry
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DNA-dependent DNA polymerase pattern in noninfected and herpesvirus infected rabbit kidney cells.

1973

In this paper we report on a DNA-dependent DNA polymerase produced in herpesvirus infected cells which is not present in virions. It differs from the polymerases of noninfected cells by its molecular weight as well as by its insensitivity to cytosine arabinoside triphosphate (ara-CTP).

medicine.medical_specialtyDNA polymerasevirusesDeoxyribonucleotidesKidneyTritiumchemistry.chemical_compoundMedical microbiologyAdenosine TriphosphateVirologyRabbit kidneymedicineAnimalsSimplexvirusheterocyclic compoundsPolymeraseCells CulturedbiologyCell-Free SystemCytarabineGeneral Medicinebiochemical phenomena metabolism and nutritionVirologyMolecular biologyMolecular WeightchemistryDNA Nucleotidyltransferasesbiology.proteinChromatography GelRabbitsArabinofuranosylcytosine triphosphateDNAArchiv fur die gesamte Virusforschung
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