Search results for "Sequence analysis"

showing 10 items of 1349 documents

Diplopod hemocyanin sequence and the phylogenetic position of the Myriapoda

2001

Hemocyanins are copper-containing respiratory proteins of the Arthropoda that have so far been thoroughly investigated only in the Chelicerata and the Crustacea but have remained unstudied until now in the Myriapoda. Here we report the first sequence of a myriapod hemocyanin. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two distinct subunits that are arranged in a 6 x 6 native molecule. The cloned hemocyanin subunit cDNA codes of for a polypeptide of 653 amino acids (75.5 kDa) that includes a signal peptide of 18 amino acids. The sequence closely resembles that of the chelicerate hemocyanins. Molecular phylogenetic analyses reject with high statistical con…

Signal peptideDNA Complementarymedicine.medical_treatmentMolecular Sequence DataMyriapodachemical and pharmacologic phenomenaBiologycomplex mixturesEvolution MolecularSequence Analysis ProteinGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyArthropodsEcology Evolution Behavior and SystematicsPhylogenyPhylogenetic treeSequence Homology Amino Acidhemic and immune systemsHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationSpirostreptusSister groupEvolutionary biologyHemocyaninsChelicerataSequence AlignmentSpirostreptidae
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Molecular characterization of hemoglobin from the honeybee Apis mellifera

2005

Due to the prevailing importance of the tracheal system for insect respiration, hemoglobins had been considered rare exceptions in this arthropod subphylum. Here we report the identification, cloning and expression analysis of a true hemoglobin gene in the honeybee Apis mellifera (Hymenoptera). The deduced amino acid sequence covers 171 residues (19.5 kDa) and harbors all globin-typical features, including the proximal and the distal histidines. The protein has no signal peptide for transmembrane transport and was predicted to localize in the cytoplasm. The honeybee hemoglobin gene shows an ancient structure, with introns in positions B12.2 and G7.0, while most other insect globins have div…

Signal peptideInsectaPhysiologymedia_common.quotation_subjectMolecular Sequence DataInsectBiologyHemoglobinsPhylogeneticsBotanyAnimalsAmino Acid SequenceRNA MessengerGlobinGenePeptide sequencemedia_commonGeneticsBase SequencefungiIntronSequence Analysis DNABeesBiological EvolutionInsect ScienceHemoglobinJournal of Insect Physiology
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Characterization of two new cuticular genes specifically expressed during the post-ecdysial molting period in Tenebrio molitor

1998

Abstract In a previous study, we have isolated a cDNA, TM-ACP17 , coding for a post-ecdysial adult protein of Tenebrio molitor . After screening of a genomic library with TM-ACP17 , we report isolation and sequencing of TM-ACP17 gene and a new gene, TM-LPCP29 , coding for a larval–pupal protein. These two genes exhibit a common sequence of 15 nucleotides and a characteristic of most cuticular protein genes so far described: an intron interrupting the signal peptide. The deduced aa sequence of TM-LPCP29 exhibits a high percentage of Ala (26.5%) and Val (17.5%) and is highly hydrophobic. In the N-terminal part, the motif VAAPV is repeated ten times. Numerous histidine residues are present in …

Signal peptideMolecular Sequence DataGene ExpressionGenes InsectMoltingBiologyComplementary DNAGeneticsAnimalsGenomic libraryAmino Acid SequenceRNA MessengerTenebrioGeneHistidineMessenger RNAGenomeBase SequenceSequence Homology Amino AcidPupaIntronGene Expression Regulation DevelopmentalDNASequence Analysis DNAGeneral MedicineMolecular biologyGenesBiochemistryLarvaInsect ProteinsMoultingGene
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Sequence of the new Drosophila melanogaster small heat-shock-related gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5.

1995

Abstract In this study, we report the molecular cloning of a novel Drosophila melanogaster small heat-shock (HS)-homologous gene, l(2)efl, identified on the right arm of the second chromosome at locus 59F4,5. We describe the temporal expression of l(2)efl in the wild-type and present its structure. The deduced amino-acid sequence of the Efl protein shows significant homology to all known small HS proteins identified in Drosophila and vertebrates, and to mammalian α-crystallin.

Signal peptideTranscription GeneticMolecular Sequence DataRestriction MappingLocus (genetics)Genes InsectMolecular cloningHomology (biology)biology.animalSequence Homology Nucleic AcidGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerRelated geneCloning MolecularGeneHeat-Shock ProteinsIn Situ HybridizationGeneticsbiologyBase SequenceSequence Homology Amino AcidVertebrateGeneral MedicineSequence Analysis DNAbiology.organism_classificationDrosophila melanogasterInsect HormonesGenes LethalDrosophila melanogasterGene
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Characterization of a cDNA clone encoding a glycine-rich cuticular protein of Tenebrio molitor: developmental expression and effect of a juvenile hor…

1992

0962-1075 (Print) Journal Article; The complete sequence of a cDNA clone, isolated from epidermal mRNA of Tenebrio molitor using a monoclonal antibody raised against an adult-specific cuticular antigen only present in the hard cuticle, was obtained after primer extension at the 5' end. From this cDNA sequence, the deduced protein encompasses 199 amino acids (including a signal peptide) with a total molecular weight of 20.7 kDa. The protein exhibits a bipartite structure: glycine-rich region located in its NH2-terminal part and a carboxy-terminal domain sharing homologies with other cuticular proteins of Orthoptera, Diptera and Lepidoptera. In-situ hybridization analysis shows that the corre…

Signal peptideanimal structuresMethoprene/*pharmacologyCuticleMolecular Sequence DataGlycineBiologyPrimer extensionBiological/drug effects/geneticsComplete sequenceComplementary DNAGeneticsAnimalsAmino Acid SequenceCloning MolecularTenebrioTenebrio/drug effects/*genetics/growth & developmentMolecular BiologyEpidermis/chemistry/growth & developmentProteins/drug effects/*genetics/isolation & purificationchemistry.chemical_classificationMessenger RNABase SequenceMetamorphosisfungiMetamorphosis BiologicalProteinsMolecularSequence Analysis DNADNAMethopreneMolecular biologyAmino acidGlycine/*genetics/metabolismchemistryInsect ScienceJuvenile hormoneInsect ProteinsEpidermisSequence AnalysisCloning
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Missense and nonsense mutations in melanocortin 1 receptor (MC1R) gene of different goat breeds: association with red and black coat colour phenotype…

2009

Abstract Background Agouti and Extension loci control the relative amount of eumelanin and pheomelanin production in melanocytes that, in turn, affects pigmentation of skin and hair. The Extension locus encodes the melanocortin 1 receptor (MC1R) whose permanent activation, caused by functional mutations, results in black coat colour, whereas other inactivating mutations cause red coat colour in different mammals. Results The whole coding region of the MC1R gene was sequenced in goats of six different breeds showing different coat colours (Girgentana, white cream with usually small red spots in the face; Maltese, white with black cheeks and ears; Derivata di Siria, solid red; Murciano-Granad…

Silent mutationCoatlcsh:QH426-470GenotypeMolecular Sequence DataNonsense mutationPopulationMutation MissenseMELANISMBiologyPolymorphism Single NucleotideAGOUTI PROTEINSettore AGR/17 - Zootecnica Generale E Miglioramento GeneticoMSH RECEPTORBREEDSMC1RGeneticsAnimalsMissense mutationGenetics(clinical)Amino Acid Sequencecoat colour; MC1R; goatAlleleHair ColoreducationAllele frequencyPOPULATIONPOLYMORPHISMSAllelesGenetics (clinical)Geneticseducation.field_of_studySTIMULATING-HORMONE-RECEPTORGoatsgoatCATTLE BREEDSSequence Analysis DNAMolecular biologyCOAT COLORlcsh:GeneticsPhenotypeCodon NonsensePIGMENTATIONWHITEReceptor Melanocortin Type 1EXTENSIONcoat colourResearch ArticleMelanocortin 1 receptorBMC Genetics
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Quasispecies dynamics and fixation of a synonymous mutation in hantavirus transmission.

2008

RNA-dependent RNA polymerases, the key enzymes in replication of RNA viruses, have a low fidelity; thus, these viruses replicate as a swarm of mutants termed viral quasispecies. Constant generation of new mutations allows RNA viruses to adapt swiftly to a novel environment through selection of both pre-existing and de novo-generated genetic variants. Here, quasispecies dynamics were studied in vivo in controlled hantavirus transmission from experimentally infected to naïve rodents through infested cage bedding. An elementary step of virus microevolution was apparent, as one synonymous mutation (A759G) repeatedly became fixed in the viral RNA quasispecies populations in the recipient animals.

Silent mutationOrthohantavirusvirusesHantavirus InfectionsViral quasispeciesBiologyVirusEvolution Molecular03 medical and health sciencesVirologyAnimalsPolymerase030304 developmental biologyHantavirusGenetics0303 health sciences030306 microbiologyArvicolinaeRNASequence Analysis DNAbiology.organism_classificationVirology3. Good healthViral evolutionMutationbiology.proteinRNA ViralBunyaviridaeThe Journal of general virology
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Isolation and characterization of two T-box genes from sponges, the phylogenetically oldest metazoan taxon

2003

It is now well established that all metazoan phyla derived from one common ancestor, the hypothetical Urmetazoa. Due to the basal position of Porifera (Demospongiae) in the phylogenetic tree of Metazoa, studies on the mechanisms controlling the development of these animals can provide clues on the understanding of the origin of multicellular animals and on how the first organization of the body plan evolved. In this report we describe the isolation and genomic characterization of two T-box genes from the siliceous sponge Suberites domuncula. The phylogenetic analysis classifies one into the subfamily of Brachyury, Sd-Bra, and the second into the Tbx2 subfamily, Sd-Tbx2. Analyses of the Sd-B…

Siliceous spongeBrachyuryDNA ComplementarySubfamilyMolecular Sequence DataMolecular evolutionPhylogeneticsGeneticsAnimalsProtein IsoformsElectrophoresis Gel Two-DimensionalAmino Acid SequencePhylogenyBase SequencebiologyPhylogenetic treeSequence Analysis DNAAnatomybiology.organism_classificationPoriferaSuberites domunculaAlternative SplicingBody planEvolutionary biologyT-Box Domain ProteinsProtein Processing Post-TranslationalDevelopmental BiologyDevelopment Genes and Evolution
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A systems biology perspective on cholangiocellular carcinoma development: focus on MAPK-signaling and the extracellular environment.

2008

Background/Aims Multiple genes have been implicated in cholangiocellular carcinoma (CCC) development. However, the overall neoplastic risk is likely associated with a much lower number of critical physiological pathways. Methods To investigate this hypothesis, we extracted all published genetic associations for the development of CCC from PubMed (genetic association studies, but also studies associating genes and CCC in general, i.e. functional studies in cell lines, genetic studies in humans, knockout mice etc.) and integrated CCC microarray data. Results We demonstrated the MAPK pathway was consistently enriched in CCC. Comparing our data to genetic associations in HCC often successfully …

SorafenibMAPK/ERK pathwayNiacinamideMAP Kinase Signaling SystemPyridinesSystems biologyAntineoplastic AgentsOncogenomicsBiologyCholangiocarcinomaMiceDatabases GeneticmedicineAnimalsHumansGeneOligonucleotide Array Sequence AnalysisHepatologyMicroarray analysis techniquesKinasePhenylurea CompoundsSystems BiologyBenzenesulfonatesComputational BiologySorafenibBiological EvolutionBile Ducts IntrahepaticBile Duct NeoplasmsMultigene FamilyImmunologyKnockout mouseCancer researchExtracellular Spacemedicine.drugJournal of hepatology
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Neuroglobin, cytoglobin, and myoglobin contribute to hypoxia adaptation of the subterranean mole rat Spalax.

2010

The subterranean mole rat Spalax is an excellent model for studying adaptation of a mammal toward chronic environmental hypoxia. Neuroglobin (Ngb) and cytoglobin (Cygb) are O 2 -binding respiratory proteins and thus candidates for being involved in molecular hypoxia adaptations of Spalax . Ngb is expressed primarily in vertebrate nerves, whereas Cygb is found in extracellular matrix-producing cells and in some neurons. The physiological functions of both proteins are not fully understood but discussed with regard to O 2 supply, the detoxification of reactive oxygen or nitrogen species, and apoptosis protection. Spalax Ngb and Cygb coding sequences are strongly conserved. However, mRNA and …

SpalaxNeuroglobinNerve Tissue ProteinsBiologyRats Sprague-DawleyExtracellularAnimalsHumansGlobinHypoxiaRegulation of gene expressionMessenger RNAMultidisciplinaryBase SequenceMyoglobinCytoglobinCytoglobinAnatomySequence Analysis DNABiological Sciencesbiology.organism_classificationAdaptation PhysiologicalCell biologyGlobinsRatsGene Expression RegulationApoptosisNeuroglobinSpalaxProceedings of the National Academy of Sciences of the United States of America
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