Search results for "Amino acid sequence"

showing 10 items of 1296 documents

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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Rat adrenoleukodystrophy-related (ALDR) gene: full-length cDNA sequence and new insight in expression.

2001

X-linked adrenoleukodystrophy (X-ALD) is an inherited demyelinating disorder due to mutations in the ALD gene, which encodes a peroxisomal ABC half-transporter (ALDP). It has been suggested that ALDP assembles with ALDRP (adrenoleukodystrophy-related protein), a close homologous half-transporter, to form a functional heterodimer. For the first time full-length ALDRP cDNA (5.5 kb) was cloned, and 5' and 3' RACE analysis revealed that alternative usage of polyadenylation sites generates the two transcripts of 3.0 and 5.5 kb observed in the rat in Northern blot analysis. Southern blotting and chromosomal mapping demonstrated one ALDR locus in the rat genome. Characterisation of the 3' flanking…

DNA ComplementaryPolyadenylationMolecular Sequence DataBiophysicsLocus (genetics)BiologyATP Binding Cassette Transporter Subfamily DBiochemistryMiceFenofibrateStructural BiologyComplementary DNAGene expressionGeneticsmedicineAnimalsNorthern blotAmino Acid SequenceCloning MolecularRats WistarAdrenoleukodystrophyGene3' Untranslated RegionsSouthern blotGene LibraryGeneticsBase SequenceBrainChromosome MappingGene Expression Regulation DevelopmentalProteinsmedicine.diseaseMolecular biologyRatsProtein BiosynthesisAdrenoleukodystrophyATP-Binding Cassette Transporters5' Untranslated RegionsBiochimica et biophysica acta
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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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Retinoid X receptor and retinoic acid response in the marine sponge Suberites domuncula

2003

SUMMARY To date no nuclear receptors have been identified or cloned from the phylogenetically oldest metazoan phylum, the Porifera (sponges). We show that retinoic acid causes tissue regression in intact individuals of the demosponge Suberites domuncula and in primmorphs, special three-dimensional cell aggregates. Primmorphs were cultivated on a galectin/poly-L-lysine matrix in order to induce canal formation. In the presence of 1 or 50 μmol l–1 retinoic acid these canals undergo regression, a process that is reversible. We also cloned the cDNA from S. domunculaencoding the retinoid X receptor (RXR), which displays the two motifs of nuclear hormone receptors, the ligand-binding and the DNA-…

DNA ComplementaryRetinoid X receptor; Suberites domuncula; marine spongesCroatiaReceptors Retinoic AcidPhysiologyMolecular Sequence DataRetinoic acidGene ExpressionApoptosisEnzyme-Linked Immunosorbent AssayTretinoinRetinoic acid receptor betaAquatic ScienceRetinoic acid-inducible orphan G protein-coupled receptorchemistry.chemical_compoundAnimalsCluster AnalysisAmino Acid SequenceMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsbiologySequence Analysis DNARetinoic acid receptor gammaBlotting Northernbiology.organism_classificationRetinoid X receptor gammaPoriferaCell biologySuberites domunculaRetinoic acid receptorRetinoid X ReceptorschemistryBiochemistryRetinoic acid receptor alphaInsect ScienceAnimal Science and ZoologySequence AlignmentTranscription FactorsJournal of Experimental Biology
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Identification of a novel Drosophila melanogaster gene, angel, a member of a nested gene cluster at locus 59F4,5.

1996

The identification of a novel Drosophila melanogaster gene, angel, is presented in this study. angel is located on the right arm of the second chromosome at locus 59F5, close to the nested genes l(2)tid, l(2)not, l(2)rot and l(2)dtl. We describe the genetic and molecular localization of angel and present its temporal expression in the wild-type. The deduced amino acid sequence of the ANG39 protein is characterized by a nuclear localization signal. Furthermore, the central part of the predicted ANG39 protein shows significant homology to the C-terminal portion of the yeast transcriptional effector CCR4.

DNA ComplementarySaccharomyces cerevisiae ProteinsMolecular Sequence DataRestriction MappingBiophysicsLocus (genetics)Genes InsectBiochemistryHomology (biology)ChromosomesFungal ProteinsRibonucleasesStructural BiologyGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceCloning MolecularGenePeptide sequenceGeneticsbiologyBase SequenceEffectorChromosome MappingGene Expression Regulation Developmentalbiology.organism_classificationBlotting NorthernNested geneDrosophila melanogasterMultigene FamilyInsect ProteinsDrosophila melanogasterSequence AlignmentNuclear localization sequenceTranscription FactorsBiochimica et biophysica acta
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Cloning and expression of a cDNA copy of the viral K28 killer toxin gene in yeast

1995

The killer toxin K28, secreted by certain killer strains of the yeast Saccharomyces cerevisiae is genetically encoded by a 1.9 kb double-stranded RNA, M-dsRNA (M28), that is present within the cell as a cytoplasmically inherited virus-like particle (VLP). For stable maintenance and replication, M28-VLPs depend on a second dsRNA virus (LA), which has been shown to encode the major capsid protein (cap) and a capsid-polymerase fusion protein (cap-pol) that provides the toxin-coding M-satellites with their transcription and replicase functions. K28 toxin-coding M28-VLPs were isolated, purified and used in vitro for the synthesis of the single-stranded M28 transcript, which was shown to be of pl…

DNA ComplementarySaccharomyces cerevisiae ProteinsTranscription GeneticMolecular Sequence DataGene ExpressionRNA-dependent RNA polymeraseSaccharomyces cerevisiaeBiologyOpen Reading FramesTranscription (biology)Complementary DNAGene expressionGeneticsAmino Acid SequenceCloning MolecularProtein PrecursorsMolecular BiologyGeneRNA Double-StrandedBase SequenceSequence Analysis RNANucleic acid sequenceRNARNA FungalDNA-Directed RNA PolymerasesSequence Analysis DNAMycotoxinsMolecular biologyKiller Factors YeastOpen reading frameProtein BiosynthesisNucleic Acid ConformationRNA ViralMolecular and General Genetics MGG
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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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Structure of MHC class I and class II cDNAs and possible immunodeficiency linked to class II expression in the Mexican axolotl

1998

Despite the fact that the axolotl (Ambystoma spp. a urodele amphibian) displays a large T-cell repertoire and a reasonable B-cell repertoire, its humoral immune response is slow (60 days), non-anamnestic, with a unique IgM class. The cytotoxic immune response is slow as well (21 days) with poor mixed lymphocyte reaction stimulation. Therefore, this amphibian can be considered as immunodeficient. The reason for this subdued immune response could be an altered antigenic presentation by major histocompatibility complex (MHC) molecules. This article summarizes our work on axolotl MHC genes. Class I genes have been characterized and the cDNA sequences show a good conservation of non-polymorphic …

DNA ComplementarySequence analysisGenes MHC Class IIMolecular Sequence DataImmunologyGenes MHC Class IPeptide bindingMajor histocompatibility complexEpitopeAntigenAxolotlMHC class IAnimalsHumansImmunology and AllergyAmino Acid SequenceRNA MessengerGeneticsPolymorphism GeneticBase SequencebiologyHistocompatibility Antigens Class IIbiology.organism_classificationAmbystoma mexicanumbiology.proteinAlpha chainImmunological Reviews
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