Search results for "Rhodopsins"

showing 10 items of 18 documents

Food Sensation Modulates Locomotion by Dopamine and Neuropeptide Signaling in a Distributed Neuronal Network

2018

Finding food and remaining at a food source are crucial survival strategies. We show how neural circuits and signaling molecules regulate these food-related behaviors in Caenorhabditis elegans. In the absence of food, AVK interneurons release FLP-1 neuropeptides that inhibit motorneurons to regulate body posture and velocity, thereby promoting dispersal. Conversely, AVK photoinhibition promoted dwelling behavior. We identified FLP-1 receptors required for these effects in distinct motoneurons. The DVA interneuron antagonizes signaling from AVK by releasing cholecystokinin-like neuropeptides that potentiate cholinergic neurons, in response to dopaminergic neurons that sense food. Dopamine al…

0301 basic medicineCell signalingSensory Receptor CellsInterneuronDopamineSensationNeuropeptideOptogeneticsBiologyReceptors DopamineAnimals Genetically Modified03 medical and health sciencesChannelrhodopsinsDopamineNeural PathwaysBiological neural networkmedicineAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGeneral NeuroscienceNeuropeptidesdigestive oral and skin physiologyDopaminergicOptogenetics030104 developmental biologymedicine.anatomical_structureFoodDopamine receptorCalciumNeuroscienceLocomotionmedicine.drugNeuron
researchProduct

Assessing sensory versus optogenetic network activation by combining (o)fMRI with optical Ca2+ recordings

2016

Encoding of sensory inputs in the cortex is characterized by sparse neuronal network activation. Optogenetic stimulation has previously been combined with fMRI (ofMRI) to probe functional networks. However, for a quantitative optogenetic probing of sensory-driven sparse network activation, the level of similarity between sensory and optogenetic network activation needs to be explored. Here, we complement ofMRI with optic fiber-based population Ca2+ recordings for a region-specific readout of neuronal spiking activity in rat brain. Comparing Ca2+ responses to the blood oxygenation level-dependent signal upon sensory stimulation with increasing frequencies showed adaptation of Ca2+ transient…

0301 basic medicineGenetic VectorsPopulationOptogenetic fMRIChannelrhodopsinSensory systemStimulationOptogeneticsSomatosensory system03 medical and health sciences0302 clinical medicineChannelrhodopsinsTransduction GeneticBiological neural networkAnimalseducationEvoked PotentialsOptical FibersNeuronseducation.field_of_studyAniline CompoundsSensory stimulation therapyChemistrySomatosensory CortexOriginal Articlesoptical neurophysiologyFluoresceinsMagnetic Resonance ImagingRats Inbred F344calcium recordingsOptogeneticsOxygen030104 developmental biologyMicroscopy FluorescenceNeurologylight propagationCalciumFemalesparse network activationNeurology (clinical)Cardiology and Cardiovascular MedicineNeurosciencePhotic Stimulation030217 neurology & neurosurgeryJournal of Cerebral Blood Flow & Metabolism
researchProduct

Potential Second-Harmonic Ghost Bands in Fourier Transform Infrared (FT-IR) Difference Spectroscopy of Proteins

2018

Fourier transform infrared (FT-IR) difference absorption spectroscopy is a common method for studying the structural and dynamical aspects behind protein function. In particular, the 2800–1800 cm−1 spectral range has been used to obtain information about internal (deuterated) water molecules, as well as site-specific details about cysteine residues and chemically modified and artificial amino acids. Here, we report on the presence of ghost bands in cryogenic light-induced FT-IR difference spectra of the protein bacteriorhodopsin. The presence of these ghost bands can be particularly problematic in the 2800–1900 cm−1 region, showing intensities similar to O–D vibrations from water molecules…

0301 basic medicineMaterials scienceAbsorption spectroscopyInfraredAnalytical chemistryInfrared spectroscopy010402 general chemistry01 natural sciences03 medical and health sciencessymbols.namesakeSpectroscopy Fourier Transform InfraredFourier transform infrared spectroscopySpectroscopyInstrumentationSpectroscopybiologyProteinsBacteriorhodopsin0104 chemical sciences030104 developmental biologyApplied spectroscopyFourier transformBacteriorhodopsinssymbolsbiology.proteinArtifactsApplied Spectroscopy
researchProduct

pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin

2017

Infrared spectroscopy has been used in the past to probe the dynamics of internal proton transfer reactions taking place during the functional mechanism of proteins but has remained mostly silent to protonation changes in the aqueous medium. Here, by selectively monitoring vibrational changes of buffer molecules with a temporal resolution of 6 µs, we have traced proton release and uptake events in the light-driven proton-pump bacteriorhodopsin and correlate these to other molecular processes within the protein. We demonstrate that two distinct chemical entities contribute to the temporal evolution and spectral shape of the continuum band, an unusually broad band extending from 2,300 to well…

0301 basic medicineModels MolecularCytoplasmNuclear TheoryMolecular ConformationInfrared spectroscopyIonic bondingProtonationBuffers010402 general chemistry53001 natural sciences03 medical and health sciencesDeprotonationSpectroscopy Fourier Transform InfraredMoleculeNuclear ExperimentMultidisciplinarybiologyChemistryWaterBacteriorhodopsinHydrogen-Ion Concentration0104 chemical sciencesKinetics030104 developmental biologyPNAS PlusChemical physicsCytoplasmTemporal resolutionBacteriorhodopsinsbiology.proteinPhysics::Accelerator PhysicsProtonsMetabolic Networks and PathwaysProtein Binding
researchProduct

Reconstitution of bacteriorhodopsin and ATP synthase from Micrococcus luteus into liposomes of the purified main tetraether lipid from Thermoplasma a…

1995

The archaebacterium Thermoplasma acidophilum is cultivated at 59 degrees C in a medium containing sulfuric acid of pH 2. The purified bipolar membrane spanning main phospholipid (MPL) of this organism can be used to produce stable liposomes of 100-500 nm in diameter either using a French pressure cell detergent dialysis or sonication. Despite a potassium diffusion potential of 186 mV very low ionic permeability of sonicated MPL liposomes was measured using the potassium binding fluorescent indicator benzofuran isophthalate PBF1, which measures net K+ uptake. The latter also remained very low, in the presence of the K(+) ionophore valinomycin and palmitic acid. Addition of valinomycin and th…

Carbonyl Cyanide p-TrifluoromethoxyphenylhydrazoneLightOctoxynolThermoplasmaBiochemistryPermeabilityPyranineValinomycinchemistry.chemical_compoundAdenosine TriphosphateProton transportParticle SizeMolecular BiologyPhospholipidsLiposomeChromatographyValinomycinbiologyIonophoresVesicleOrganic ChemistryFatty AcidsTemperatureThermoplasma acidophilumMembrane ProteinsPhospholipid EthersBacteriorhodopsinCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationMicrococcus luteusProton-Translocating ATPaseschemistryBacteriorhodopsinsLiposomesbiology.proteinGramicidinPotassiumProtonsChemistry and physics of lipids
researchProduct

Key roles for freshwater A ctinobacteria revealed by deep metagenomic sequencing

2014

Freshwater ecosystems are critical but fragile environments directly affecting society and its welfare. However, our understanding of genuinely freshwater microbial communities, constrained by our capacity to manipulate its prokaryotic participants in axenic cultures, remains very rudimentary. Even the most abundant components, freshwater Actinobacteria, remain largely unknown. Here, applying deep metagenomic sequencing to the microbial community of a freshwater reservoir, we were able to circumvent this traditional bottleneck and reconstruct de novo seven distinct streamlined actinobacterial genomes. These genomes represent three new groups of photoheterotrophic, planktonic Actinobacteria.…

DNA BacterialMolecular Sequence DatarhodopsinsFresh WaterCyanobacteria633 - Cultivos y producciones [CDU]GenomeFreshwater ecosystemActinobacteriaContig MappingPhylogeneticsRNA Ribosomal 16Slignin degradationGeneticsMicrococcineaePhylogenyEcology Evolution Behavior and SystematicsmetagenomicsbiologyEcologyHigh-Throughput Nucleotide SequencingSequence Analysis DNAbiology.organism_classificationfreshwater reservoirActinobacteriaSpainMetagenomicsMetagenomicsActinomycetalesWater MicrobiologyGenome BacterialGC-contentMolecular Ecology
researchProduct

Interfacial water structure controls protein conformation.

2007

A phenomenological theory of salt-induced Hofmeister phenomena is presented, based on a relation between protein solubility in salt solutions and protein-water interfacial tension. As a generalization of previous treatments, it implies that both kosmotropic salting out and chaotropic salting in are manifested via salt-induced changes of the hydrophobic/hydrophilic properties of protein-water interfaces. The theory is applied to describe the salt-dependent free energy profiles of proteins as a function of their water-exposed surface area. On this basis, three classes of protein conformations have been distinguished, and their existence experimentally demonstrated using the examples of bacter…

DYNAMICSMECHANISMKosmotropicProtein ConformationSURFACE-TENSIONSurface tensionchemistry.chemical_compoundProtein structureMaterials ChemistryPhysical and Theoretical ChemistryPURPLE MEMBRANESPECTROSCOPYbiologySTABILITYBACTERIORHODOPSINMyoglobinSALTTemperatureWaterBacteriorhodopsinSTABILITY MECHANISMSurfaces Coatings and FilmsION SPECIFICITYChaotropic agentCrystallographyMyoglobinchemistryTEMPERATURE-DEPENDENCEChemical physicsStructural stabilityBacteriorhodopsinsbiology.proteinSalting outThermodynamicsThe journal of physical chemistry. B
researchProduct

The effect of water on protein dynamics

2004

Neutron diffraction and spectroscopy were applied to describe the hydration and dynamics of a soluble protein and a natural membrane from extreme halophilic Archaea. The quantitative dependence of protein motions on water activity was clearly illustrated, and it was established that a minimum hydration shell is required for the systems to access their functional resilience, i.e. a dynamics state that allows biological activity.

Dynamical transitionWater activityNeutron diffractionHalophilic malate dehydrogenaseBacteriorhodopsinHydration shellNeutronEuryarchaeotaGeneral Biochemistry Genetics and Molecular BiologyMalate DehydrogenaseSpectroscopySpectrum AnalysibiologyChemistrySpectrum AnalysisProtein dynamicsWaterBacteriorhodopsinPurple membraneAgricultural and Biological Sciences (miscellaneous)Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Neutron DiffractionMembraneSolvation shellAgricultural and Biological Sciences (all)BiochemistryChemical physicsBacteriorhodopsinsbiology.proteinBacteriorhodopsinsGeneral Agricultural and Biological SciencesResearch ArticlePhilosophical Transactions of the Royal Society of London. Series B: Biological Sciences
researchProduct

Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

2012

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…

Halobacterium salinarumModels MolecularProtein FoldingProtein Denaturation01 natural sciencesBiotecnologiaBiochemistryBiophysics Simulationschemistry.chemical_compoundSensory RhodopsinsHalobacterium salinarum0303 health sciencesMultidisciplinarybiologyProtein StabilityQRTemperatureUltraviolet-visible spectroscopyThermal stabilityBacterial BiochemistryChemistryBiochemistryBacteriorhodopsinsRetinaldehydeMedicineProtonsResearch ArticleSteric effectsHydrogen bondingBioquímicaProtein StructureScienceRetinal bindingBiophysics010402 general chemistryMicrobiologyPhosphates03 medical and health sciencesBiology030304 developmental biologyAspartic AcidBinding SitesAdaptation OcularOrganic ChemistryOrganic SynthesisProteinsChromoproteinsRetinalBacteriorhodopsinBacteriologyBiological TransportChromophorebiology.organism_classification0104 chemical sciencesTransmembrane ProteinschemistryRetinaldehydeBiophysicsbiology.proteinMutant ProteinsPLoS ONE
researchProduct

Coreconstitution of bacterial ATP synthase with monomeric bacteriorhodopsin into liposomes. A comparison between the efficiency of monomeric bacterio…

1987

The conditions for coreconstitution of a bacterial ATP synthase and bacteriorhodopsin into lecithin liposomes and for light driven ATP synthesis have been optimized. A rate of maximally 280 nmol ATP min-1 mg ATP synthase-1 was achieved with monomerized bacteriorhodopsin compared with a rate of up to 45 nmol ATP min-1 mg-1 found for proteoliposomes containing bacteriorhodopsin in the form of purple membrane patches. The different rates are explained by the finding that monomeric bacteriorhodopsin is more homogeneously distributed among the liposomes than the purple membrane patches. The final activities depended on both the purification method for the two proteins and the coreconstitution pr…

Liposomefood.ingredientLightATP synthasebiologyChemiosmosisKineticsBacteriorhodopsinRhodospirillum rubrumBiochemistryLecithinKineticsProton-Translocating ATPaseschemistry.chemical_compoundMonomerfoodMembranechemistryBiochemistryBacteriorhodopsinsLiposomesbiology.proteinEuropean Journal of Biochemistry
researchProduct