Search results for " AMINO"

showing 10 items of 789 documents

Tonoplast subcellular localization of maize cytochrome b5 reductases

2000

Plant cytochrome b 5 reductases (b 5 R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b 5 ) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. Here we report on cDNA cloning of a novel maize b 5 R, NFR II, strongly related to a previously cloned cDNA, NFR I (Bagnaresi et al., 1999, Biochem, J. 338, 499-5051. Maize b 5 R isoforms are produced by a small multi-gene family. The NFR cDNAs were shown to encode active b 5 Rs by heterologous expression in yeast. Both reductases, in addition to Fe 3+ -chelates, efficiently reduced Cu 2+ -chelates. Using a polyclonal antibody able to recogniz…

DNA ComplementaryMolecular Sequence DataSaccharomyces cerevisiaePlant ScienceMolecular cloningBiologyPlant RootsZea maysIsozymeGene Expression Regulation EnzymologicComplementary DNACytochrome b5GeneticsAmino Acid SequenceMicroscopy ImmunoelectronCytochrome ReductasesCytochrome b5 reductaseSequence Homology Amino AcidCytochrome bSequence Analysis DNACell BiologySubcellular localizationMolecular biologyIsoenzymesBiochemistryVacuolesHeterologous expressionSequence AlignmentCytochrome-B(5) ReductaseThe Plant Journal
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Identification of a gene overexpressed in aphids reared under short photoperiod.

2003

Most aphids develop a cyclic parthenogenesis life-cycle. After several generations of viviparously produced parthenogenetic females, follows a single annual generation of sexual individuals, usually in autumn, that mate and lay the sexual eggs. Shortening of photoperiod at the end of the summer (together with temperature) is a key factor inducing the sexual response. Currently no genes involved in the cascade of events that lead to the appearance of sexual forms have been reported. After a Differential Display RT-PCR survey performed on Acyrthosiphon pisum aphids, we identified a gene that is overexpressed in aphids reared under short photoperiod conditions that induce sexuality in this spe…

DNA ComplementaryPhotoperiodMolecular Sequence DataBiologyBiochemistrySexual Behavior AnimalComplementary DNAAnimalsCircadian rhythmAmino Acid SequenceCloning MolecularMolecular BiologyGeneDNA PrimersphotoperiodismGeneticsDifferential displayBase SequenceSequence Homology Amino Acidfood and beveragesParthenogenesisbiology.organism_classificationAcyrthosiphon pisumInsect ScienceAphidsGABAergicInsect ProteinsInsect biochemistry and molecular biology
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γ-Tubulin in Barley and Tobacco: Sequence Relationship and RNA Expression Patterns in Developing Leaves during Mitosis and Post-Mitotic Growth

2002

gamma-Tubulin is typically associated with microtubule organising centres, such as the centrosome, and appears to mediate microtubule nucleation. Centrosomes are usually not found in higher plants, but active genes homologous to gamma-tubulin have been identified in the plant kingdom, including the angiosperms Arabidopsis, maize and rice. We have isolated and characterised gamma-tubulin cDNA sequences of two further angiosperm species, barley and tobacco. Sequence comparison revealed a phylogenetic tree with distinct clusters corresponding to the systematic position of the species. Furthermore, domains, thought to be exposed in the folded protein and to be candidates for interaction with as…

DNA ComplementaryPhysiologyMolecular Sequence DataMitosismacromolecular substancesPlant ScienceGene Expression Regulation PlantTubulinMicrotubuleTobaccoAmino Acid SequenceGeneMitosisPhylogenyMicrotubule nucleationGeneticsSequence Homology Amino AcidbiologyGene Expression Regulation Developmentalfood and beveragesRNAHordeumCell BiologyGeneral MedicineBlotting NorthernCell biologyPlant LeavesTubulinRNA PlantCentrosomebiology.proteinCortical microtubulePlant and Cell Physiology
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Putative phenoloxidases in the tunicate Ciona intestinalis and the origin of the arthropod hemocyanin superfamily.

2003

In addition to the respiratory copper-containing proteins for which it is named, the arthropod hemocyanin superfamily also includes phenoloxidases and various copperless storage proteins (pseudo-hemocyanins, hexamerins and hexamerin receptors). It had long been assumed that these proteins are restricted to the arthropod phylum. However, in their analysis of the predicted genes in the Ciona intestinalis (Urochordata:Tunicata) genome, Dehal et al. (Science 298:2157–2167) proposed that the sea squirt lacks hemoglobin but uses hemocyanin for oxygen transport. While there are, nevertheless, four hemoglobin genes present in Ciona, we have identified and cloned two cDNA sequences from Ciona that i…

DNA ComplementaryPhysiologymedicine.medical_treatmentMolecular Sequence Datachemical and pharmacologic phenomenacomplex mixturesBiochemistryEvolution MolecularEndocrinologyPhylogeneticsmedicineAnimalsCiona intestinalisAmino Acid SequenceArthropodsEcology Evolution Behavior and SystematicsPhylogenybiologyBase SequenceSequence Homology Amino AcidMonophenol MonooxygenaseOxygen transportHemocyaninAnatomybiology.organism_classificationCiona intestinalisCionaEvolutionary biologyHemocyaninsAnimal Science and ZoologyArthropod ProteinsArthropodOxygen bindingJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Identification, molecular cloning, and phylogenetic analysis of a non-respiratory pseudo-hemocyanin of Homarus americanus.

1999

Copper-containing hemocyanins serve to transport oxygen in many arthropod species. Here I describe the identification and cDNA cloning of a structurally closely related non-respiratory pseudo-hemocyanin (PHc) of the American lobster, Homarus americanus. This protein has lost the ability to bind copper and, therefore, oxygen because a histidine residue in copper-binding site A is replaced by tyrosine. Like many arthropod hemocyanins, PHc forms a hexamer. It consists of two different subunit types of 660 and 661 amino acids, respectively, that share a 94.4% sequence identity. Whereas Homarus hemocyanin is produced in the hepatopancreas, PHc is synthesized by the ovaries and the heart tissue. …

DNA ComplementaryProtein subunitmedicine.medical_treatmenteducationMolecular Sequence Datachemical and pharmacologic phenomenaMolecular cloningBiologybehavioral disciplines and activitiesBiochemistryPhylogeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequencePhylogenychemistry.chemical_classificationHomarusBase SequenceSequence Homology Amino AcidEcologyHemocyaninCell BiologyProtein superfamilybiology.organism_classificationAmino acidNephropidaeMicroscopy ElectronBiochemistrychemistryHemocyaninsThe Journal of biological chemistry
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Tumor suppression inDrosophila is causally related to the function of thelethal(2)tumorous imaginal discs gene, adnaJ homolog

1995

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) causes in homozygotes malignant growth of cells of the imaginal discs and the death of the mutant larvae at the time of puparium formation. We describe the molecular cloning of the l(2)tid+ gene and its temporal expression pattern in the wild-type and mutant alleles. Germ line rescue of the tumor phenotype was achieved with a 7.0 kb Hindlll-fragment derived from the polytene chromosome band 59F5. The l(2)tid+ gene spans approximately 2.5 kb of genomic DNA. The protein coding region, 1,696 bps long, is divided by an intron into two exons. The predicted Tid56 protein contains 518 amino acids and posse…

DNA ComplementarySaccharomyces cerevisiae ProteinsTumor suppressor geneMolecular Sequence DataMutantGenes InsectSaccharomyces cerevisiaeAnimals Genetically ModifiedFungal ProteinsMitochondrial ProteinsSpecies SpecificityEscherichia coliGeneticsAnimalsDrosophila ProteinsHumansGenes Tumor SuppressorAmino Acid SequenceCloning MolecularGeneAllelesHeat-Shock ProteinsPolytene chromosome bandBase SequenceSequence Homology Amino AcidbiologyEscherichia coli ProteinsPupaChromosome MappingExonsNeoplasms ExperimentalCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyImaginal discDrosophila melanogasterLarvaDNAJA2Drosophila melanogasterSequence AlignmentDrosophila ProteinDevelopmental BiologyDevelopmental Genetics
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Molecular cloning and characterization of aCandida albicansgene (EFB1) coding for the elongation factor EF-1β

1996

A Candida albicans gene homologous to Saccharomyces cerevisiae elongation factor 1 beta was isolated by screening a genomic DNA library using a C. albicans cDNA as a probe. This cDNA was previously obtained by immunoscreening of an expression library with polyclonal antibodies raised against candidal cell wall components. Sequence analysis of the cDNA and the whole C. albicans gene (EMBL accession number X96517) revealed an intron-interrupted open reading frame of 639 base pairs that encodes a 213 amino acid protein. Exon sequences are highly homologous (74%) to S. cerevisiae EFB1, whereas intron sequence is less conserved (34% identity), and the predicted amino acid sequence shares about 7…

DNA ComplementarySequence analysisGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeMolecular cloningMicrobiologyFungal ProteinsPeptide Elongation Factor 1ImmunoscreeningComplementary DNACandida albicansGeneticsAnimalsCloning MolecularCandida albicansMolecular BiologyPeptide sequenceGeneGeneticsGenomeBase SequenceSequence Homology Amino AcidbiologySequence Analysis DNABlotting NorthernPeptide Elongation Factorsbiology.organism_classificationMolecular biologyElongation factorBlotting SouthernRabbitsFEMS Microbiology Letters
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Arbutin synthase, a novel member of the NRD1β glycosyltransferase family, is a unique multifunctional enzyme converting various natural products and …

2002

Plant glucosyltransferases (GTs) play a crucial role in natural product biosynthesis and metabolization of xenobiotics. We expressed the arbutin synthase (AS) cDNA from Rauvolfia serpentina cell suspension cultures in Escherichia coli with a 6 x His tag and purified the active enzyme to homogeneity. The recombinant enzyme had a temperature optimum of 50 degrees C and showed two different pH optima (4.5 and 6.8 or 7.5, depending on the buffer). Out of 74 natural and synthetic phenols and two cinnamyl alcohols tested as substrates for the AS, 45 were accepted, covering a broad range of structural features. Converting rates comparable to hydroquinone were not achieved. In contrast to this broa…

DNA ComplementaryStereochemistryMolecular Sequence DataClinical BiochemistryPharmaceutical ScienceBiochemistryRauwolfiaSubstrate SpecificityXenobioticschemistry.chemical_compoundGlucosyltransferasesBiosynthesisMultienzyme ComplexesDrug DiscoveryGlycosyltransferaseGlycosylAmino Acid SequenceCloning MolecularMolecular BiologyPhylogenychemistry.chemical_classificationBiological ProductsBase SequenceSequence Homology Amino AcidbiologyOrganic ChemistryArbutinArbutinTemperatureGlycosyltransferasesSubstrate (chemistry)Hydrogen-Ion ConcentrationRecombinant ProteinsKineticsEnzymeBiochemistrychemistrybiology.proteinMolecular MedicineGlucosyltransferaseSequence AlignmentBioorganic & Medicinal Chemistry
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Plant progesterone 5β-reductase is not homologous to the animal enzyme. Molecular evolutionary characterization of P5βR from Digitalis purpurea

2007

Plants of the genus Digitalis produce cardiac glycosides, i.e. digoxin, which are widely used for congestive heart failure. Progesterone 5beta-reductase (P5betaR) is a key enzyme in the biosynthesis of these natural products. Here, we have carried out the purification and partial amino acid sequencing of the native P5betaR from foxglove (Digitalis purpurea), and isolated a cDNA encoding this enzyme. Similarly to other steroid 5beta-reductases, the recombinant P5betaR catalyzes the stereospecific reduction of the Delta(4)-double bond of several steroids with a 3-oxo,Delta(4,5) structure. The gene encoding P5betaR is expressed in all plant organs, and maximally transcribed in leaves and matur…

DNA ComplementarySubfamilyRecombinant Fusion ProteinsMolecular Sequence DataPlant ScienceHorticultureReductaseBiochemistryGas Chromatography-Mass SpectrometryEvolution Molecularchemistry.chemical_compoundPhylogeneticsComplementary DNACardenolideAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenyProgesteronePlant Proteinschemistry.chemical_classificationGeneticsDigitalisBase SequenceMolecular StructureSequence Homology Amino AcidbiologyProgesterone ReductaseReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingDigitalis purpureaGeneral Medicinebiology.organism_classificationEnzymeModels ChemicalBiochemistrychemistryElectrophoresis Polyacrylamide GelPhytochemistry
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Different genomic organization and expression of immunoglobulin light-chain isotypes in the rainbow trout.

2000

cDNA studies have distinguished two isotypes of the rainbow trout (Oncorhynchus mykiss) immunoglobulin (Ig) light chain (designated L1 and L2). This study characterized genomic clones of these isotypes. L1 genes are arranged in clusters with single copies of variable (V), joining (J), and constant (C) segments. The transcriptional orientation of the V genes is opposite to that of the J and C segments, indicating that the V genes must be rearranged by inversion. L2 is also organized in clusters, consisting of two or three V, one J, and one C exon, all in the same transcriptional orientation. L1 and L2 of rainbow trout are similar to the previously identified cod and catfish clusters. Repeat …

DNA ComplementaryTATA boxImmunologyMolecular Sequence DataImmunoglobulin Variable RegionGene ExpressionBiologyImmunoglobulin light chainComplementary DNASequence Homology Nucleic AcidGeneticsAnimalsAmino Acid SequenceRNA MessengerEnhancerPromoter Regions GeneticGeneGenomic organizationGeneticsBase SequenceSequence Homology Amino AcidMolecular biologyImmunoglobulin IsotypesRegulatory sequenceOncorhynchus mykissImmunoglobulin Joining RegionImmunoglobulin Light ChainsSequence motifImmunoglobulin Constant RegionsImmunogenetics
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