Search results for "sequence data"

showing 10 items of 1952 documents

The transcription reinitiation properties of RNA polymerase III in the absence of transcription factors

2007

AbstractTranscription reinitiation by RNA polymerase (Pol) III proceeds through facilitated recycling, a process by which the terminating Pol III, assisted by the transcription factors TFIIIB and TFIIIC, rapidly reloads onto the same transcription unit. To get further insight into the Pol III transcription mechanism, we analyzed the kinetics of transcription initiation and reinitiation of a simplified in vitro transcription system consisting only of Pol III and template DNA. The data indicates that, in the absence of transcription factors, first-round transcription initiation by Pol III proceeds at a normal rate, while facilitated reinitiation during subsequent cycles is compromised.

RNA polymerase IIISaccharomyces cerevisiae ProteinsTranscription GeneticvirusesShort CommunicationMolecular Sequence DataRNA polymerase IISaccharomyces cerevisiaeBiochemistryRNA polymerase IIITranscription Factor TFIIIBTranscription Factors TFIIIGene Expression Regulation FungalMolecular BiologyTFIIIBBase SequencebiologyGeneral transcription factorG-less cassetteCell BiologyMolecular biologyTranscription preinitiation complexbiology.proteinTranscription reinitiationTranscription factor II FTranscription factor II ETranscription factor II DTranscription factor II BCellular and Molecular Biology Letters
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Species- and Subtype-Specific Recognition by Antibody WF6 of a Sequence Segment Forming an α-Bungarotoxin Binding Site on the Nicotinic Acetylcholine…

1992

The monoclonal antibody WF6 competes with acetylcholine and alpha-bungarotoxin (alpha-BGT) for binding to the Torpedo nicotinic acetylcholine receptor (nAChR) alpha 1 subunit. Using synthetic peptides corresponding to the complete Torpedo nAChR alpha 1 subunit, we previously mapped a continuous epitope recognized by WF6, and the prototope for alpha-BGT, to the sequence segment alpha 1(181-200). Single amino acid substitution analogs have been used as an initial approach to determine the critical amino acids for WF6 and alpha-BGT binding. In the present study, we continue our analysis of the structural features of the WF6 epitope by comparing its cross-reactivity with synthetic peptides corr…

Ranidaealpha7 Nicotinic Acetylcholine ReceptorMolecular Sequence DataCross ReactionsReceptors NicotinicBiologyTorpedoEpitopelaw.inventionMiceSpecies SpecificityAntibody SpecificitylawSequence Homology Nucleic AcidmedicineAnimalsHumansReceptors CholinergicAmino Acid SequenceBinding sitePharmacologyMusclesBinding proteinAntibodies MonoclonalSnakesBungarotoxinsMolecular biologyRatsNicotinic acetylcholine receptorBiochemistryCattleAlpha-4 beta-2 nicotinic receptorPeptidesTorpedoAcetylcholineCys-loop receptorsmedicine.drugJournal of Receptor Research
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Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis.

2000

Monoterpenoid indole alkaloids are a vast and structurally complex group of plant secondary compounds. In contrast to other groups of plant products which produce many glycosides, indole alkaloids rarely occur as glucosides. Plants of Rauvolfia serpentina accumulate ajmaline as a major alkaloid, whereas cell suspension cultures of Rauvolfia mainly accumulate the glucoalkaloid raucaffricine at levels of 1.6 g/l. Cell cultures do contain a specific glucosidase. known as raucaffricine-O-beta-D-glucosidase (RG), which catalyzes the in vitro formation of vomilenine, a direct intermediate in ajmaline biosynthesis. Here, we describe the molecular cloning and functional expression of this enzyme in…

RauvolfiaDNA ComplementaryStereochemistryMolecular Sequence DataPlant ScienceHorticultureMolecular cloningBiochemistryIndole AlkaloidsSubstrate SpecificityMagnoliopsidaAlkaloidsRauvolfia serpentinamedicineAmino Acid SequenceCloning MolecularMolecular BiologybiologyBase SequenceGeneral Medicinebiology.organism_classificationSecologanin Tryptamine AlkaloidsAjmalineBlotting SouthernBiochemistryVomilenineStrictosidinebiology.proteinHeterologous expressionGlucosidasesGlucosidasesmedicine.drugPhytochemistry
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Hydroquinone: O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences.

2000

Plant cell suspension cultures of Rauvolfia are able to produce a high amount of arbutin by glucosylation of exogenously added hydroquinone. A four step purification procedure using anion exchange, hydrophobic interaction, hydroxyapatite-chromatography and chromatofocusing delivered in a yield of 0.5%, an approximately 390 fold enrichment of the involved glucosyltransferase. SDS-PAGE showed a M(r) for the enzyme of 52 kDa. Proteolysis of the pure enzyme with endoproteinase LysC revealed six peptide fragments with 9-23 amino acids which were sequenced. Sequence alignment of the six peptides showed high homologies to glycosyltransferases from other higher plants.

RauvolfiaStereochemistryMolecular Sequence DataPeptidePlant ScienceHorticultureBiochemistryRauwolfiachemistry.chemical_compoundRauvolfia serpentinaAmino Acid SequenceMolecular BiologyCells Culturedchemistry.chemical_classificationChromatographyPlants MedicinalbiologyChromatofocusingArbutinGeneral Medicinebiology.organism_classificationChromatography Ion ExchangePeptide FragmentsAmino acidMolecular WeightKineticsEnzymeDurapatitechemistryBiochemistryGlucosyltransferasesbiology.proteinGlucosyltransferaseElectrophoresis Polyacrylamide GelPhytochemistry
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Intermolecular Cystine-Bonding of Murine Interleukin 2 Indicates that Ligand Dimerization is Important for the Formation of the High-Affinity Recepto…

1992

Interleukin 2 is thought to be active as a monomeric protein. As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2. (3H) thymidine incorporation assays with intermolecular cystine-bonded or monomeric mIL2 revealed almost identical median effective concentrations (EC50) and high-affinity dissociation constants (Kdh), respectively. Comparative binding and internalization assays suggest that one cystine-bonded dimeric or two monomeric mIL2 molecules bind to the high-affinit…

Receptor complexStereochemistryMolecular Sequence DataClinical BiochemistrySuccinimidesLigandsCell LineMicechemistry.chemical_compoundEndocrinologyAnimalsAmino Acid SequenceReceptorPeptide sequencechemistry.chemical_classificationMolecular massLigandReceptors Interleukin-2Cell BiologyAmino acidDissociation constantKineticsCross-Linking ReagentsMonomerchemistryBiochemistryCystineInterleukin-2Cell DivisionGrowth Factors
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The N-terminal Amino Group of [Tyr8]Bradykinin Is Bound Adjacent to Analogous Amino Acids of the Human and Rat B2 Receptor

1996

To obtain data of the bradykinin B2 receptor's agonist binding site, we used a combined approach of affinity labeling and "immunoidentification" of receptor fragments generated by cyanogen bromide cleavage. Domain-specific antibodies to the various extracellular receptor domains were applied to detect receptor fragments with covalently attached [125I-Tyr8]bradykinin. As a cross-linker we used the homobifunctional reagent disuccinimidyl tartarate (DST), which reacts preferentially with primary amines. With this technique a [125I-Tyr8]bradykinin-labeled receptor fragment derived from the third extracellular domain was identified. The epsilon-amino group of lysine (Lys172) of the human B2 rece…

Receptor Bradykinin B2StereochemistryAffinity labelMolecular Sequence DataBradykininBradykininTransfectionBiochemistryProtein Structure SecondaryCell LineIodine Radioisotopeschemistry.chemical_compoundAnimalsHumansAmino Acid SequenceBradykinin receptorReceptorMolecular BiologyPeptide sequencechemistry.chemical_classificationBinding SitesAffinity labelingbiologyLysineReceptors BradykininAffinity LabelsCell BiologyRecombinant ProteinsRatsAmino acidCross-Linking ReagentschemistryBiochemistryCOS CellsFree fatty acid receptorbiology.proteinJournal of Biological Chemistry
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The unique complexity of the CYP3A4 upstream region suggests a nongenetic explanation of its expression variability.

2010

The individually variable and unpredictable expression of CYP3A4 compromises therapies with 50% of contemporary drugs. Gene variants explain only a fraction of this variability.We investigated the evolution of CYP3A4 transcriptional regulation by nuclear receptors such as the xenobiotics sensors PXR and CAR.The combination of a proximal ER6 element with XREM and CLEM represents the original scheme of CYP3A regulation by nuclear receptors in placental mammals. Among human CYP3A genes, this scheme is retained only in CYP3A4, whereas non-CYP3A4 genes lost these elements to a variable extent during primate evolution. In parallel, the number of elements outside XREM and CLEM potentially responsi…

Receptors SteroidMolecular Sequence DataReceptors Cytoplasmic and NuclearBiologyLigandsTransfectionGene Expression Regulation EnzymologicXenobioticsTranscription (biology)PhylogeneticsLuciferases FireflyGeneticsTranscriptional regulationCytochrome P-450 CYP3AHumansGeneral Pharmacology Toxicology and PharmaceuticsReceptorPromoter Regions GeneticMolecular BiologyGeneGenetics (clinical)Constitutive Androstane ReceptorRegulation of gene expressionGeneticsPregnane X receptorBinding SitesBase SequencePregnane X ReceptorNuclear receptorMolecular MedicineSequence AnalysisProtein BindingPharmacogenetics and genomics
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Species-specific mechanisms for cholesterol 7alpha-hydroxylase (CYP7A1) regulation by drugs and bile acids.

2005

The gene encoding cholesterol 7alpha-hydroxylase (CYP7A1) is tightly regulated in order to control intrahepatic cholesterol and bile acid levels. Ligands of the xenobiotic-sensing pregnane X receptor inhibit CYP7A1 expression. To retrace the evolution of the molecular mechanisms underlying CYP7A1 inhibition, we used a chicken hepatoma cell system that retains the ability to be induced by phenobarbital and other drugs. Whereas bile acids regulate CYP7A1 via small heterodimer partner and liver receptor homolog-1, mRNA expression of these nuclear receptors is unchanged by xenobiotics. Instead, drugs repress chicken hepatic nuclear factor 4alpha (HNF4alpha) transcript levels concomitant with a …

Receptors Steroidmedicine.drug_classMolecular Sequence DataBiophysicsReceptors Cytoplasmic and NuclearBiologyIn Vitro TechniquesCholesterol 7 alpha-hydroxylaseBiochemistryGene Expression Regulation EnzymologicBile Acids and SaltsMiceSpecies SpecificitymedicineAnimalsHumansRNA MessengerCholesterol 7-alpha-HydroxylaseMolecular BiologyCells CulturedMice KnockoutPregnane X receptorBile acidLiver receptor homolog-1Pregnane X ReceptorPhosphoproteinsRecombinant ProteinsDNA-Binding ProteinsBiochemistryNuclear receptorHepatocyte Nuclear Factor 4PhenobarbitalSmall heterodimer partnerHepatocytesFarnesoid X receptorSignal transductionChickensSignal TransductionTranscription FactorsArchives of biochemistry and biophysics
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Development of type-specific and cross-reactive serological probes for the minor capsid protein of human papillomavirus type 33.

1993

Human papillomavirus type 33 (HPV33) is associated with malignant tumors of the cervix. In an attempt to develop immunological probes for HPV33 infections, antisera against various bacterial fusion proteins carrying sequences of the minor capsid protein encoded by L2 were raised in animals. Antigenic determinants on the HPV33 L2 protein were identified by using truncated fusion proteins and were classified as type specific or cross-reactive with respect to HPV1, -8, -11, -16, and -18. Cross-reactive epitopes map to amino acids 98 to 107 or to amino acids 102 to 112 and 107 to 117, respectively, depending on the fusion protein used for immunization. Antibodies directed toward these epitopes …

Recombinant Fusion ProteinsImmunologyGuinea PigsMolecular Sequence DataPeptideBiologyMicrobiologyEpitopeStructure-Activity RelationshipCapsidAntigenSpecies SpecificityVirologyAnimalsAmino Acid SequenceStaphylococcal Protein APeptide sequenceAntigens ViralPapillomaviridaeGlutathione TransferaseSequence Deletionchemistry.chemical_classificationBase SequenceOncogene Proteins Viralbeta-GalactosidaseMolecular biologyFusion proteinAmino acidchemistryCapsidOligodeoxyribonucleotidesInsect Sciencebiology.proteinCapsid ProteinsRabbitsAntibodySequence AlignmentResearch ArticleJournal of virology
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In vivo Trafficking and Localization of p24 Proteins in Plant Cells

2008

p24 proteins constitute a family of putative cargo receptors that traffic in the early secretory pathway. p24 proteins can be divided into four subfamilies (p23, p24, p25 and p26) by sequence homology. In contrast to mammals and yeast, most plant p24 proteins contain in their cytosolic C-terminus both a dilysine motif in the -3, -4 position and a diaromatic motif in the -7, -8 position. We have previously shown that the cytosolic tail of Arabidopsis p24 proteins has the ability to interact with ARF1 and coatomer (through the dilysine motif) and with COPII subunits (through the diaromatic motif). Here, we establish the localization and trafficking properties of an Arabidopsis thaliana p24 pr…

Recombinant Fusion ProteinsMolecular Sequence DataArabidopsisGolgi ApparatusVacuoleProtein Sorting SignalsBiologyEndoplasmic ReticulumBiochemistrysymbols.namesakeStructural BiologyArabidopsisGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceMolecular BiologyCOPIISecretory pathwayArabidopsis ProteinsLysineEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusbiology.organism_classificationActinsCell biologyDNA-Binding ProteinsProtein TransportBiochemistryCoatomerVacuolessymbolsCOP-Coated VesiclesCarrier ProteinsTranscription FactorsTraffic
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