Search results for "G proteins"

showing 10 items of 992 documents

The peroxisome proliferator response element (PPRE) present at positions -681/-669 in the rat liver 3-ketoacyl-CoA thiolase B gene functionally inter…

2000

Although previous data showed that the putative thiolase B PPRE located at -681/-669 bind the PPARalpha-RXRalpha heterodimer in vitro (Kliewer et al. (1992) Nature 358, 771-774), there is no evidence about the functional role of this element. By gel mobility-shift assay, we found an interaction of this PPRE with not only PPARalpha but also with HNF-4. By transfection of cells with the putative PPRE-driven luciferase reporter vector and PPARalpha, we found no significant activation of the luciferase gene expression, in contrast to the case with reporter expression driven by the PPRE of the peroxisomal bifunctional enzyme. On the other hand, HNF-4 activated the luciferase gene expression driv…

Response elementBiophysicsReceptors Cytoplasmic and NuclearBiologyTransfectionBiochemistryDNA-binding proteinPeroxisomal Bifunctional EnzymeGenes ReporterGene expressionAnimalsMolecular BiologyGeneDNA PrimersBase SequenceThiolaseCell BiologyTransfectionDNAAcetyl-CoA C-AcyltransferasePhosphoproteinsMolecular biologyRatsDNA-Binding ProteinsHepatocyte nuclear factor 4Hepatocyte Nuclear Factor 4LiverCOS CellsPeroxisome ProliferatorsTranscription FactorsBiochemical and biophysical research communications
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In situ localization of the Antennapedia gene on the chromosomes of nine Drosophila species of the obscura group.

2008

The homeotic Antennapedia gene, cloned from the genomic DNA of D. subobscura, was localized on the polytene chromosomes of nine species of the Drosophila obscura group. In all of them, the probe used hybridized on chromosomes equivalent to the E element of Muller's terminology. These results are consistent with the idea that single copy genes do not move around the genome and that chromosomal elements have conserved their genetic identity during evolution.

Restriction MappingAntennapediaGenomeGene mappingSpecies SpecificityGeneticsAnimalsDrosophila ProteinsDrosophila (subgenus)GeneGeneticsHomeodomain ProteinsPolytene chromosomebiologyNuclear ProteinsGeneral MedicineThoraxbiology.organism_classificationBiological EvolutionChromosome BandingDNA-Binding ProteinsAntennapedia Homeodomain ProteinDrosophilaDrosophila obscuraHomeotic geneDNA ProbesTranscription FactorsHereditas
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Cloning of a novel putative G-protein-coupled receptor (NLR) which is expressed in neuronal and lymphatic tissue.

1993

AbstractA novel G-protein-coupled receptor was isolated from mouse and rat neuronal and lymphatic tissues. The amino acid sequence of the rat receptor (rNLR) shows an overall homology of 80% to a recently cloned receptor from Burkitt's lymphoma cells (BLR1) which is exclusively expressed in lymphatic tissues [(1992) Eur. J. Immunol. 22, 2795]. Much less homology between rNLR and BLR1 was observed at the N-terminus (about 40%), whereas rNLR and the mouse homologue mNLR show 92% amino acid identity. Northern blot analysis of NLR revealed a predominant 5.5 kb mRNA species in various brain regions and neuronal cell lines, whereas in the spleen a 3 kb transcript is predominant. This distribution…

Restriction MappingInterleukin 8BiochemistryReceptors G-Protein-CoupledMiceStructural BiologyTumor Cells CulturedLymphocytesCloning MolecularReceptorPeptide sequencechemistry.chemical_classificationNeuronsGenomic LibraryBurkitt's lymphomaBrainBurkitt LymphomaPolymerase chain reactionAmino acidOligodeoxyribonucleotidesOrgan SpecificityG-protein-coupled receptorBLR1Molecular Sequence DataBiophysicsReceptors Cell SurfaceBiologyNLRGTP-Binding ProteinsComplementary DNAGeneticsmedicineAnimalsHumansNorthern blotAmino Acid SequenceRNA MessengerMolecular BiologyG protein-coupled receptorMessenger RNABase SequenceSequence Homology Amino AcidCell Biologymedicine.diseaseMolecular biologyIntronsRatsNG108-15 cellchemistryBurkitt's lymphomaFEBS letters
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Connecting temporal identity to mitosis: the regulation of Hunchback in Drosophila neuroblast lineages.

2006

Both in vertebrates and invertebrates, neural stem cells generate different cell types at different times during development. It has been suggested that this process depends on temporal identity transitions of neural progenitors, but the underlying mechanism has not been resolved, yet. Recently, Drosophila neuroblasts (NBs) have been shown to be an excellent model system to investigate this subject. Here, changes in temporal identity are regulated by sequential and transient expression of transcription factors in the NB, such as Hunchback (Hb) and Kruppel (Kr). The temporal expression profile is maintained in the progeny. Hb is expressed first and thus defines the earliest identity in a giv…

Retinal Ganglion CellsCell typeReceptors SteroidKruppel-Like Transcription FactorsDown-RegulationMitosisNerve Tissue ProteinsBiologyCell fate determinationKrüppelNeuroblastAnimalsDrosophila ProteinsNuclear export signalMolecular BiologyMitosisTranscription factorGeneticsNeuronsModels GeneticNuclear ProteinsCell DifferentiationCell BiologyNeural stem cellDNA-Binding ProteinsProtein BiosynthesisDrosophilaDevelopmental BiologyTranscription FactorsCell cycle (Georgetown, Tex.)
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Molecular genetics of autosomal dominant retinitis pigmentosa (ADRP): a comprehensive study of 43 Italian families

2005

Retinitis pigmentosa is the most common form of retinal degeneration and is heterogeneous both clinically and genetically. The autosomal dominant forms ( ADRP) can be caused by mutations in 12 different genes. This report describes the first simultaneous mutation analysis of all the known ADRP genes in the same population, represented by 43 Italian families. This analysis allowed the identification of causative mutations in 12 of the families (28% of the total). Seven different mutations were identified, two of which are novel (458delC and 6901C --> T (P2301S), in the CRX and PRPF8 genes, respectively). Several novel polymorphisms leading to amino acid changes in the FSCN2, NRL, IMPDH1, and…

Retinal degenerationDNA Mutational Analysismedicine.disease_causeGene FrequencyPrevalenceAge of OnsetSPLICING-FACTOR GENESChildGenetics (clinical)Genes DominantGeneticsMutationeducation.field_of_studyRNA-Binding ProteinsMiddle AgedDNA-Binding ProteinsBasic-Leucine Zipper Transcription FactorsItalyChild PreschoolMESSENGER-RNAMicrotubule-Associated ProteinsRetinitis PigmentosaFORMAdultRhodopsinmedicine.medical_specialtycongenital hereditary and neonatal diseases and abnormalitiesAdolescentPopulationRHODOPSIN GENEBiologyMolecular geneticsRetinitis pigmentosaGeneticsmedicineHumansFamilyEye ProteinseducationGeneAllele frequencyHomeodomain ProteinsMUTATIONSmedicine.diseaseeye diseasesMutationTrans-ActivatorsMutation testingOnline Mutation ReportCarrier Proteins
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Plasma Proteins, Yolk Proteins and Metal-Binding Proteins

1994

The extracellular fluid of the metazoans is not only a transport vehicle but also, for the majority of the body’s cells, their growth environment. Proteins play an important role here, providing colloid-osmotic pressure and acting as buffers. The most important parameter in this respect is their concentration which, depending upon the species, the developmental stage and the physiological conditions, can vary from less than 1 to more than 200 mg/ml (Table 5.1). In addition to these general functions, individual plasma proteins have various specific roles, e.g. in the transport of substances, in defence reactions, in blood clotting or in the solution of clots. At least in the case of the mor…

Retinol binding proteinMembrane proteinAntifreeze proteinChemistryExtracellular fluidExtracellularBiophysicsMetal binding proteinsPlant lipid transfer proteinsBlood proteins
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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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Differential expression and interaction with the visual G-protein transducin of centrin isoforms in mammalian photoreceptor cells.

2004

Photoisomerization of rhodopsin activates a heterotrimeric G-protein cascade leading to closure of cGMP-gated channels and hyperpolarization of photoreceptor cells. Massive translocation of the visual G-protein transducin, Gt, between subcellular compartments contributes to long term adaptation of photoreceptor cells. Ca(2+)-triggered assembly of a centrin-transducin complex in the connecting cilium of photoreceptor cells may regulate these transducin translocations. Here we demonstrate expression of all four known, closely related centrin isoforms in the mammalian retina. Interaction assays revealed binding potential of the four centrin isoforms to Gtbetagamma heterodimers. High affinity b…

Rhodopsingenetic structuresLightBlotting WesternBiologyBiochemistryRetinaRats Sprague-DawleyMiceCalcium-binding proteinHeterotrimeric G proteinmedicineAnimalsProtein IsoformsScattering RadiationCiliaTransducinMicroscopy ImmunoelectronMolecular BiologyCyclic GMPGlutathione TransferaseCentrosomeRetinaChromatographyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionCiliumCalcium-Binding ProteinsCell BiologySequence Analysis DNARod Cell Outer SegmentRecombinant ProteinsCell biologyRatsMice Inbred C57BLKineticsProtein Transportmedicine.anatomical_structureMicroscopy FluorescenceRhodopsinCentrosomeCentrinbiology.proteinCalciumCattleElectrophoresis Polyacrylamide Gelsense organsTransducinProtein BindingThe Journal of biological chemistry
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DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair

2016

Abstract Repair of damaged DNA relies on the recruitment of DNA repair factors in a well orchestrated manner. As a prerequisite, the chromatin needs to be decondensed by chromatin remodelers to allow for binding of repair factors and for DNA repair to occur. Recent studies have implicated members of the SWI/SNF and INO80 families as well as PARP1 in nucleotide excision repair (NER). In this study, we report that the endonuclease DICER is implicated in chromatin decondensation during NER. In response to UV irradiation, DICER is recruited to chromatin in a ZRF1-mediated manner. The H2A–ubiquitin binding protein ZRF1 and DICER together impact on the chromatin conformation via PARP1. Moreover, …

Ribonuclease III0301 basic medicineDNA RepairUltraviolet RaysDNA damageDNA repairgenetic processesPoly (ADP-Ribose) Polymerase-1Genome Integrity Repair and ReplicationBiologyChromatin remodelingCell LineDEAD-box RNA HelicasesHistones03 medical and health scienceschemistry.chemical_compoundUbiquitinCell Line TumorGeneticsAnimalsHumansCaenorhabditis elegansOncogene ProteinsOsteoblastsUbiquitinfungiRNA-Binding ProteinsFibroblastsChromatin Assembly and DisassemblyMolecular biologyChromatinChromatinDNA-Binding Proteinsenzymes and coenzymes (carbohydrates)HEK293 Cells030104 developmental biologychemistrybiology.proteinDNADNA DamageMolecular ChaperonesNucleotide excision repairDicerNucleic Acids Research
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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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