Search results for "MELANOGASTER"

showing 10 items of 452 documents

Cell cycle independent role of Cyclin E during neural cell fate specification in Drosophila is mediated by its regulation of Prospero function

2009

AbstractDuring development, neural progenitor cells or neuroblasts generate a great intra- and inter-segmental diversity of neuronal and glial cell types in the nervous system. In thoracic segments of the embryonic central nervous system of Drosophila, the neuroblast NB6-4t undergoes an asymmetric first division to generate a neuronal and a glial sublineage, while abdominal NB6-4a divides once symmetrically to generate only 2 glial cells. We had earlier reported a critical function for the G1 cyclin, CyclinE (CycE) in regulating asymmetric cell division in NB6-4t. Here we show that (i) this function of CycE is independent of its role in cell cycle regulation and (ii) the two functions are m…

ProsperoNerve Tissue ProteinsStem cellsCyclinEBiologyCell fate determinationNeuroblastNeuroblastsCyclin EAsymmetric cell divisionAnimalsDrosophila ProteinsCell LineageMolecular BiologyNeural cellCell ProliferationSequence DeletionNeuronsCell fate determinationCell CycleNuclear ProteinsCell DifferentiationCell BiologyCell cycleNeural stem cellUp-RegulationCell biologyProtein TransportDrosophila melanogasternervous systemDrosophilaCNSStem cellGanglion mother cellBiomarkersProtein BindingTranscription FactorsDevelopmental BiologyDevelopmental Biology
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Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin

2005

Hemoglobins at high concentration have been isolated long ago from some insect larvae living in hypoxic environments. Conversely, a monomeric hemoglobin has been discovered recently in the fruit fly Drosophila melanogaster as intracellular protein expressed both in larvae and in the adult fly. Such a finding indicates that the oxygen supply in insects may be more complex than previously thought, relying not only on O2 diffusion through the tubular tracheal system, but also on carrier-mediated transport and storage. We present here the crystal structure of recombinant D. melanogaster hemoglobin at 1.20 A resolution. Spectroscopic data show that the protein displays a hexacoordinated heme, wh…

Protein ConformationHemeMatrix (biology)BiologyCrystallography X-RayLigandsBiochemistrylaw.inventionchemistry.chemical_compoundHemoglobinslawMelanogasterAnimalsDrosophila ProteinsHistidineMolecular BiologyHemeCyclohexylaminesBinding SitesSpectrum AnalysisfungiCell BiologyHEXAbiology.organism_classificationOxygenMyoglobinchemistryBiochemistryAlkanesulfonic AcidsBiophysicsRecombinant DNAHemoglobinDrosophila melanogaster
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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Choice alters Drosophila oviposition site preference on menthol

2013

Summary Food choice and preference relies on multiple sensory systems that are under the control of genes and sensory experience. Exposure to specific nutrients and nutrient-related molecules can change food preference in vertebrates and invertebrates. For example, larval exposure of several holometabolous insects to menthol can change their adult response to this molecule. However, studies involving Drosophila melanogaster exposure to menthol produced controversial results due maybe to methodological differences. Here, we compared the oviposition-site preference of wild-type D. melanogaster lines freely or forcibly exposed to menthol-rich food. After 12 generations, oviposition-site prefer…

QH301-705.5Science[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionZoologymentholBiology[ SDV.BA ] Life Sciences [q-bio]/Animal biologyaversive behaviourFood preferenceegg-laying behaviour;aversive behaviour;menthol;caffeine;sucroseGeneral Biochemistry Genetics and Molecular BiologyToxicologychemistry.chemical_compoundBiologie animaleFood choiceMelanogasterFood and NutritionBiology (General)DrosophilacaffeineAnimal biologyLarva[SDV.BA]Life Sciences [q-bio]/Animal biologyQfungisucrosebiology.organism_classificationPreferenceegg-laying behaviourchemistryAlimentation et NutritionDrosophila melanogasterGeneral Agricultural and Biological SciencesMenthol[SDV.AEN]Life Sciences [q-bio]/Food and NutritionResearch Article
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In developing Drosophila neurones the production of γ-amino butyric acid is tightly regulated downstream of glutamate decarboxylase translation and c…

2003

The presented work pioneers the embryonic Drosophila CNS for studies of the developmental regulation and function of gamma-amino butyric acid (GABA). We describe for the first time the developmental pattern of GABA in Drosophila and address underlying regulatory mechanisms. Surprisingly, and in contrast to vertebrates, detectable levels of GABA occur late during Drosophila neurogenesis, after essential neuronal proliferation and growth have taken place and synaptogenesis has been initiated. This timeline is almost unchanged when the GABA synthetase glutamate decarboxylase (GAD) is strongly misexpressed throughout the nervous system suggesting a tight post-translational regulation of GABA ex…

Regulation of gene expressionNervous systemNeurogenesisGlutamate decarboxylaseSynaptogenesisTranslation (biology)Biologybiology.organism_classificationBiochemistryCellular and Molecular Neurosciencemedicine.anatomical_structureBiochemistrymedicineNeuronDrosophila melanogasterJournal of Neurochemistry
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Mapping and structure of DMXL1, a human homologue of the DmX gene from Drosophila melanogaster coding for a WD repeat protein.

2000

The DmX gene was recently isolated from the X chromosome of Drosophila melanogaster. TBLASTN searches of the dbEST databases revealed sequences with a high level of similarity to DmX in a variety of different species, including insects, nematodes, and mammals showing that DmX is an evolutionarily highly conserved gene. Here we describe the cloning of the cDNA and the chromosomal localization of one of the human homologues of DmX, Dmx-like 1 (DMXL1). The human DMXL1 gene codes for a large mRNA of 11 kb with an open reading frame of 3027 amino acids. The putative protein belongs to the superfamily of WD repeat proteins, which have mostly regulatory functions. The DMXL1 protein contains an exc…

Repetitive Sequences Amino AcidDNA ComplementaryMolecular Sequence DataBiologyConserved sequenceMiceGene mappingComplementary DNAGeneticsAnimalsDrosophila ProteinsHumansRadiation hybrid mappingAmino Acid SequenceDinucleotide RepeatsGeneIn Situ Hybridization FluorescenceGeneticsBase SequenceChromosome MappingProteinsbiology.organism_classificationOpen reading frameDrosophila melanogasterChromosomes Human Pair 5Insect ProteinsDrosophila melanogasterDrosophila ProteinGenomics
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Gypsy endogenous retrovirus maintains potential infectivity in several species of Drosophilids.

2008

Abstract Background Sequences homologous to the gypsy retroelement from Drosophila melanogaster are widely distributed among drosophilids. The structure of gypsy includes an open reading frame resembling the retroviral gene env, which is responsible for the infectious properties of retroviruses. Results In this study we report molecular and phylogeny analysis of the complete env gene from ten species of the obscura group of the genus Drosophila and one species from the genus Scaptomyza. Conclusion The results indicate that in most cases env sequences could produce a functional Env protein and therefore maintain the infectious capability of gypsy in these species.

RetroelementsEvolutionvirusesGenome InsectEndogenous retrovirusSequence alignmentGenes InsectGenes envEvolution MolecularOpen Reading FramesViral Envelope ProteinsPhylogeneticsDrosophilidaeQH359-425AnimalsDrosophilidaeRNA MessengerDrosophila (subgenus)Cloning MolecularGeneEcology Evolution Behavior and SystematicsPhylogenyGeneticsLikelihood FunctionsbiologyModels GeneticReverse Transcriptase Polymerase Chain ReactionEndogenous RetrovirusesDNASequence Analysis DNAbiology.organism_classificationOpen reading frameProtein BiosynthesisDrosophila melanogasterSequence AlignmentResearch ArticleBMC evolutionary biology
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The GTP- and Phospholipid-Binding Protein TTD14 Regulates Trafficking of the TRPL Ion Channel in Drosophila Photoreceptor Cells

2015

Recycling of signaling proteins is a common phenomenon in diverse signaling pathways. In photoreceptors of Drosophila, light absorption by rhodopsin triggers a phospholipase Cβ-mediated opening of the ion channels transient receptor potential (TRP) and TRP-like (TRPL) and generates the visual response. The signaling proteins are located in a plasma membrane compartment called rhabdomere. The major rhodopsin (Rh1) and TRP are predominantly localized in the rhabdomere in light and darkness. In contrast, TRPL translocates between the rhabdomeral plasma membrane in the dark and a storage compartment in the cell body in the light, from where it can be recycled to the plasma membrane upon subsequ…

RhodopsinCancer Researchlcsh:QH426-470LightGTP'BiologyEye03 medical and health sciencesTransient receptor potential channelTransient Receptor Potential Channels0302 clinical medicineGTP-binding protein regulatorsGTP-Binding ProteinsGeneticsAnimalsDrosophila ProteinsMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsIon channel030304 developmental biology0303 health sciencesCell MembraneMembrane ProteinsDarknessRhabdomereTransport proteinCell biologylcsh:GeneticsProtein TransportDrosophila melanogasterMembrane proteinRhodopsinMutationbiology.proteinPhotoreceptor Cells Invertebrate030217 neurology & neurosurgerySignal TransductionResearch ArticlePLOS Genetics
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Chromatin-associated RNA interference components contribute to transcriptional regulation in Drosophila

2009

RNA interference (RNAi) pathways have evolved as important modulators of gene expression that operate in the cytoplasm by degrading RNA target molecules through the activity of short (21-30 nucleotide) RNAs1-6. RNAi components have been reported to have a role in the nucleus, as they are involved in epigenetic regulation and heterochromatin formation(7-10). However, although RNAi-mediated post-transcriptional gene silencing is well documented, the mechanisms of RNAi-mediated transcriptional gene silencing and, in particular, the role of RNAi components in chromatin dynamics, especially in animal multicellular organisms, are elusive. Here we show that the key RNAi components Dicer 2 (DCR2) a…

Ribonuclease IIIanimal structuresRNA-induced transcriptional silencingTranscription GeneticRNA-induced silencing complexBiology03 medical and health sciences0302 clinical medicineRNA interferenceTranscriptional regulationAnimalsDrosophila ProteinsHSP70 Heat-Shock ProteinsPromoter Regions Genetic030304 developmental biologyRNA Double-StrandedGenetics0303 health sciencesMultidisciplinaryfungiRNARNA-Binding ProteinsChromatinChromatinRNA silencingMicroRNAsDrosophila melanogasterGene Expression RegulationArgonaute ProteinsRNA InterferenceRNA Polymerase II030217 neurology & neurosurgeryDrosophila ProteinHeat-Shock ResponseRNA HelicasesProtein BindingTranscription Factors
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The complete set of ribosomal proteins from the marine sponge Suberites domuncula

2005

The siliceous marine sponge Suberites domuncula is a member of the most ancient and simplest extant phylum of multicellular animals-Porifera, which have branched off first from the common ancestor of all Metazoa. We have determined primary structures of 79 ribosomal proteins (r-proteins) from S. domuncula: 32 proteins from the small ribosomal subunit and 47 proteins from the large ribosomal subunit. Only L39 and L41 polypeptides (51 and 25 residues long in rat, respectively) are missing. The sponge S. domuncula is, after nematode Caenorhabditis elegans and insect Drosophila melanogaster the third representative of invertebrates with known amino acid sequences of all r-proteins. The comparis…

Ribosomal ProteinsSequence Homology Amino AcidbiologyPorifera; ribosome; metazoan r-proteins; SSU proteins; LSU proteins; evolutionSaccharomyces cerevisiaeGeneral Medicinebiology.organism_classificationRibosomeRatsEvolution MolecularSuberites domunculaSpongeBiochemistrySequence Analysis ProteinRibosomal proteinLarge ribosomal subunitBotanyGeneticsMelanogasterAnimalsDrosophila melanogasterSuberitesRibosomes
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