Search results for "Transferases"

showing 10 items of 426 documents

Expression of a reporter gene is reduced by a ribozyme in transgenic plants

1994

A chimeric gene encoding a ribozyme under the control of the cauliflower mosaic virus (CaMV) 35S promoter was introduced into transgenic tobacco plants. In vivo activity of this ribozyme, which was designed to cleave npt mRNA, was previously demonstrated by transient expression assays in plant protoplasts. The ribozyme gene was transferred into transgenic tobacco plants expressing an rbcS-npt chimeric gene as an indicator. Five double transformants out of sixteen exhibited a reduction in the amount of active NPT enzyme. To measure the amount of ribozyme produced, in the absence of its target, the ribozyme and target genes were separated by genetic segregation. The steady-state concentration…

TransgeneDrug ResistanceChimeric geneGene Expression Regulation PlantGenes ReporterTobaccoGene expressionGeneticsRNA CatalyticRNA MessengerPromoter Regions GeneticMolecular BiologyGeneRegulation of gene expressionReporter geneKanamycin KinasebiologyRibozymePlants Genetically Modifiedbiology.organism_classificationMolecular biologyPhosphotransferases (Alcohol Group Acceptor)Plants ToxicGene Targetingbiology.proteinCauliflower mosaic virusMolecular and General Genetics MGG
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Retrotransposon silencing and telomere integrity in somatic cells of Drosophila depends on the cytosine-5 methyltransferase DNMT2

2009

Here we show that the cytosine-5 methyltransferase DNMT2 controls retrotransposon silencing in Drosophila somatic cells. In Drosophila, significant DNMT2-dependent DNA methylation occurs during early embryogenesis. Suppression of white gene silencing by Mt2 (Dnmt2) null mutations in variegated P[w(+)] element insertions identified functional targets of DNMT2. The enzyme controls DNA methylation at retrotransposons in early embryos and initiates histone H4K20 trimethylation catalyzed by the SUV4-20 methyltransferase. In somatic cells, loss of DNMT2 eliminates H4K20 trimethylation at retrotransposons and impairs maintenance of retrotransposon silencing. In Dnmt2 and Suv4-20 null genotypes, re…

Transposable elementDNA-Cytosine MethylasesEmbryo NonmammalianMethyltransferaseRetroelementsSomatic cellRetrotransposonGene Knockout TechniquesDrosophilidaeGeneticsAnimalsDrosophila ProteinsGene silencingDNA (Cytosine-5-)-MethyltransferasesGene SilencingCrosses GeneticIn Situ Hybridization FluorescenceGeneticsbiologyfungifood and beveragesHistone-Lysine N-MethyltransferaseDNA MethylationTelomerebiology.organism_classificationTelomereMutationDrosophilaDrosophila melanogasterNature Genetics
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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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Mycobacterium tuberculosis secretory proteins downregulate T cell activation by interfering with proximal and downstream T cell signalling events

2015

Background Mycobacterium tuberculosis (M. tuberculosis) modulates host immune response, mainly T cell responses for its own survival leading to disease or latent infection. The molecules and mechanisms utilized to accomplish immune subversion by M. tuberculosis are not fully understood. Understanding the molecular mechanism of T cell response to M. tuberculosis is important for development of efficacious vaccine against TB. Methods Here, we investigated effect of M. tuberculosis antigens Ag85A and ESAT-6 on T cell signalling events in CD3/CD28 induced Peripheral blood mononuclear cells (PBMCs) of PPD+ve healthy individuals and pulmonary TB patients. We studied CD3 induced intracellular calc…

TuberculosisT-LymphocytesT cellCD3Upstream and downstream (transduction)ImmunologyIntracellular SpaceReceptors Antigen T-CellLymphocyte ActivationMycobacterium tuberculosisBacterial ProteinsCD28 AntigensmedicineHumansAntigens BacterialNFATC Transcription FactorsbiologyT-cell receptorNF-kappa BCD28hemic and immune systemsNFATMycobacterium tuberculosismedicine.diseasebiology.organism_classificationmedicine.anatomical_structureImmunologyLeukocytes Mononuclearbiology.proteinCalciumMitogen-Activated Protein KinasesAcyltransferasesResearch ArticleSignal TransductionBMC Immunology
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NMR structure of a non-conjugatable, ADP-ribosylation associated, ubiquitin-like domain from Tetrahymena thermophila polyubiquitin locus.

2019

Abstract Background Ubiquitin-like domains (UbLs), in addition to being post-translationally conjugated to the target through the E1-E2-E3 enzymatic cascade, can be translated as a part of the protein they ought to regulate. As integral UbLs coexist with the rest of the protein, their structural properties can differ from canonical ubiquitin, depending on the protein context and how they interact with it. In this work, we investigate T.th-ubl5, a UbL present in a polyubiquitin locus of Tetrahymena thermophila, which is integral to an ADP-ribosyl transferase protein. Only one other co-occurrence of these two domains within the same protein has been reported. Methods NMR, multiple sequence al…

UBL DOMAINspektroskopiaGTPasePARKINBiochemistryPROTEIN BACKBONEACTIVATIONprotein-protein interaction0302 clinical medicineProtein-protein interactionUbiquitinmolekyylidynamiikkaNMR-spektroskopiaPolyubiquitinADP Ribose Transferases0303 health sciencesMultiple sequence alignmentbiologyFERM domainChemistryTetrahymenastructure-function relationshipFAMILYCell biologyRECEPTORSPost-translational modificationSignal TransductionBiophysicsSequence alignmentMolecular Dynamics SimulationUbiquitin-like domainsMECHANISMSProtein–protein interactionTetrahymena thermophila03 medical and health sciencesNMR spectroscopyADP-RibosylationubikitiinitMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologyMolecular dynamics simulationsStructure-function relationshipmolecular dynamics simulationsbiology.organism_classificationProtein Structure Tertiarypost-translational modificationProteasomeMOLECULAR-DYNAMICSbiology.protein1182 Biochemistry cell and molecular biologyproteiinitGTPASEProtein Processing Post-Translational030217 neurology & neurosurgeryFERM DOMAINBiochimica et biophysica acta. General subjects
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UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii.

1996

Abstract We have previously isolated a fibroblast mutant cell with high resistance to the two Rho-modifying glucosyltransferase toxins A and B of Clostridium difficile. We demonstrate here a low level of UDP-glucose in the mutant, which explains its toxin resistance since: (i) to obtain a detectable toxin B-mediated Rho modification in lysates of mutant cells, addition of UDP-glucose was required, and it promoted the Rho modification dose-dependently; (ii) high pressure liquid chromatography analysis of nucleotide extracts of cells indicated that the level of UDP-glucose in the mutant (0.8 nmol/106 cells) was lower than in the wild type (3.7 nmol/106 cells); and (iii) sensitivity to toxin B…

Uridine Diphosphate GlucoseMicroinjectionsMutantBacterial ToxinsClostridium difficile toxin AClostridium sordelliiClostridium difficile toxin Bmedicine.disease_causeBiochemistryMicrobiologyCell LineCricetulusBacterial ProteinsGTP-Binding ProteinsCricetinaemedicineAnimalsMolecular BiologyClostridiumbiologyToxinClostridioides difficileWild typeCell BiologyClostridium difficilebiology.organism_classificationGlucosyltransferasesMutationbiology.proteinGlucosyltransferaseThe Journal of biological chemistry
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Phosphatidylinositol phosphate kinase type I gamma regulates dynamics of large dense-core vesicle fusion.

2005

Phosphatidylinositol-4,5-bisphosphate was proposed to be an important regulator of large dense-core vesicle exocytosis from neuroendocrine tissues. Here, we have examined the kinetics of secretion in chromaffin cells from mice lacking phosphatidylinositol phosphate kinase type Iγ, the major neuronal phosphatidylinositol-4-phosphate 5-kinase. Absence of this enzyme caused a reduction of the readily releasable vesicle pool and its refilling rate, with a small increase in morphologically docked vesicles, indicating a defect in vesicle priming. Furthermore, amperometry revealed a delay in fusion pore expansion. These results provide direct genetic evidence for a key role of phosphatidylinositol…

Vesicle fusionChromaffin CellsBiologyIn Vitro TechniquesMembrane FusionExocytosisExocytosischemistry.chemical_compoundMiceAnimalsPhosphatidylinositolCells CulturedMultidisciplinaryVesicleSecretory VesiclesSNAP25Munc-18Kiss-and-run fusionBiological SciencesSecretory VesicleCell biologyKineticsMicroscopy ElectronPhosphotransferases (Alcohol Group Acceptor)chemistryCalciumProceedings of the National Academy of Sciences of the United States of America
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Sortase A: An ideal target for anti-virulence drug development

2014

Sortase A is a membrane enzyme responsible for the anchoring of surface-exposed proteins to the cell wall envelope of Gram-positive bacteria. As a well-studied member of the sortase subfamily catalysing the cell wall anchoring of important virulence factors to the surface of staphylococci, enterococci and streptococci, sortase A plays a critical role in Gram-positive bacterial pathogenesis. It is thus considered a promising target for the development of new anti-infective drugs that aim to interfere with important Gram-positive virulence mechanisms, such as adhesion to host tissues, evasion of host defences, and bio fi lm formation. The additional properties of sortase A as an enzyme that i…

Virulence FactorsIn silicoVirulenceBiologyGram-Positive BacteriaAntimicrobial resistanceSettore BIO/19 - Microbiologia GeneraleMicrobiologyCell membraneAntibiotic resistanceGram-positive pathogenBacterial ProteinsSortaseDrug DiscoverymedicineVirulenceSortase ABiofilmAminoacyltransferasesSettore CHIM/08 - Chimica FarmaceuticaAntivirulence drugAnti-Bacterial AgentsCysteine EndopeptidasesInfectious Diseasesmedicine.anatomical_structureBiochemistryDrug developmentSortase A inhibitorSortase A
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When the nose must remain responsive: glutathione conjugation of the mammary pheromone in the newborn rabbit

2014

In insects, xenobiotic-metabolizing enzymes were demonstrated to regulate pheromones inactivation, clearing them from the olfactory periphery and keeping receptors ready for stimulation renewal. Here, we investigate whether similar processes could occur in mammals, focusing on the pheromonal communication between female rabbits and their newborns. Lactating rabbits emit in their milk a volatile aldehyde, 2-methylbut-2-enal, that elicits searching-grasping in neonates; called the mammary pheromone (MP), it is critical for pups which are constrained to find nipples within the 5 min of daily nursing. For newborns, it is thus essential to remain sensitive to this odorant during the whole nursin…

Vomeronasal organPhysiologyIngénierie des alimentsStimulationPheromonesBehavioral Neurosciencechemistry.chemical_compoundnursingnewbornODORANT-BINDING PROTEINS[SDV.IDA]Life Sciences [q-bio]/Food engineeringDinitrochlorobenzenerabbit (Oryctolagus cuniculus)EXPRESSION PATTERNSAcroleinReceptorGlutathione TransferaseGENE-EXPRESSIONglutathione transferases[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringperireceptor eventsLOCALIZATIONmammary pheromoneGlutathioneSensory SystemsSmellmedicine.anatomical_structureOrgan SpecificitySex pheromonePheromoneFemaleRabbitsENZYMESolfactionmedicine.medical_specialtyOlfactionBiologyNoseGene Expression Regulation EnzymologicPhysiology (medical)Internal medicinemedicineFood engineeringAnimalsLactationAldehydesALDEHYDEGlutathioneFeeding BehaviorUDP-GLUCURONOSYLTRANSFERASEglutathione transferases;mammary pheromone;newborn;nursing;olfaction;perireceptor events;rabbit (Oryctolagus cuniculus);xenobiotic-metabolizing enzymes;RAT OLFACTORY EPITHELIUM;ODORANT-BINDING PROTEINS;S-TRANSFERASE;UDP-GLUCURONOSYLTRANSFERASE;EXPRESSION PATTERNS;VOMERONASAL ORGAN;GENE-EXPRESSION;LOCALIZATION;ALDEHYDE;ENZYMESxenobiotic-metabolizing enzymesRAT OLFACTORY EPITHELIUMS-TRANSFERASENasal MucosaEndocrinologychemistryAnimals NewbornOlfactory epitheliumVOMERONASAL ORGAN
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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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