Search results for "PROTEIN INTERACTIONS"

showing 10 items of 52 documents

Environmental Noise and Nonlinear Relaxation in Biological Systems

2012

We analyse the effects of environmental noise in three different biological systems: (i) mating behaviour of individuals of 'Nezara viridula' (L.) (Heteroptera Pentatomidae); (ii) polymer translocation in crowded solution; (iii) an ecosystem described by a Verhulst model with a multiplicative Lèvy noise. Specifically, we report on experiments on the behavioural response of 'N. viridula' individuals to sub-threshold deterministic signals in the presence of noise. We analyse the insect response by directionality tests performed on a group of male individuals at different noise intensities. The percentage of insects which react to the sub-threshold signal shows a non-monotonic behavior, charac…

Fluctuation phenomena random processes noise and Brownian motionSettore FIS/02 - Fisica Teorica Modelli E Metodi MatematiciNoise in biological systems; Biophysical mechanisms of interaction; Fluctuation phenomena random processes noise and Brownian motion; Molecular dynamics Brownian dynamics; Molecular interactions; membrane-protein interactionsMolecular dynamics Brownian dynamicMolecular interactionNoise in biological systemmembrane-protein interactionsBiophysical mechanisms of interaction
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Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

2014

Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their …

Cancer ResearchViral proteinvirusesIntracellular SpaceBiologymedicine.disease_causeBacterial cell structureProtein–protein interactionViral Proteins03 medical and health sciencesVirologyEscherichia colimedicineBacteriophage PRD1Escherichia coli030304 developmental biology0303 health sciencesBacteria030302 biochemistry & molecular biologyDNA replicationta1182Protein interactionsFusion proteinVirus assemblyCell biologyConfocal microscopyProtein TransportInfectious DiseasesMembrane proteinVirion assemblyMembrane virusVirus Research
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11,12-EET Stimulates the Association of BK Channel α and β1 Subunits in Mitochondria to Induce Pulmonary Vasoconstriction

2012

In the systemic circulation, 11,12-epoxyeicosatrienoic acid (11,12-EET) elicits nitric oxide (NO)- and prostacyclin-independent vascular relaxation, partially through the activation of large conductance Ca(2+)-activated potassium (BK) channels. However, in the lung 11,12-EET contributes to hypoxia-induced pulmonary vasoconstriction. Since pulmonary artery smooth muscle cells also express BK channels, we assessed the consequences of BKβ(1) subunit deletion on pulmonary responsiveness to 11,12-EET as well as to acute hypoxia. In buffer-perfused mouse lungs, hypoxia increased pulmonary artery pressure and this was significantly enhanced in the presence of NO synthase (NOS) and cyclooxygenase (…

BK channelAnatomy and PhysiologyLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsRespiratory Systemlcsh:MedicineCardiovascularCardiovascular SystemBiochemistryIon ChannelsMembrane PotentialsMice81114-Eicosatrienoic AcidHypoxic pulmonary vasoconstrictionHypoxiaLarge-Conductance Calcium-Activated Potassium Channel alpha Subunitslcsh:ScienceLungEnergy-Producing OrganellesEpoxide HydrolasesMembrane Potential MitochondrialMembrane potentialMultidisciplinarybiologyChemistryDepolarizationHyperpolarization (biology)IberiotoxinMitochondriaBiochemistryCirculatory Physiologycardiovascular systemMedicinelipids (amino acids peptides and proteins)medicine.symptomResearch ArticleCell Physiologymedicine.medical_specialtyPulmonary ArteryBioenergeticsCardiovascular PharmacologyInternal medicinemedicineAnimalsHumansArterial Pressureddc:610Protein InteractionsBiologylcsh:RProteinsCalcium-activated potassium channelMice Inbred C57BLHEK293 CellsEndocrinologyVasoconstrictionbiology.proteinlcsh:QGene DeletionVasoconstrictionPLoS ONE
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µ-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptos…

2011

Anti-apoptotic Bfl-1 and pro-apoptotic Bax, two members of the Bcl-2 family sharing a similar structural fold, are classically viewed as antagonist regulators of apoptosis. However, both proteins were reported to be death inducers following cleavage by the cysteine protease µ-calpain. Here we demonstrate that calpain-mediated cleavage of full-length Bfl-1 induces the release of C-terminal membrane active α-helices that are responsible for its conversion into a pro-apoptotic factor. A careful comparison of the different membrane-active regions present in the Bfl-1 truncated fragments with homologous domains of Bax show that helix α5, but not α6, of Bfl-1 induces cell death and cytochrome c r…

Programmed cell deathProtein StructureCancer Treatmentlcsh:MedicineApoptosisMitochondrionCleavage (embryo)BiochemistryProtein Structure SecondaryMinor Histocompatibility AntigensMiceCell Line TumorMolecular Cell BiologyAnimalsHumanslcsh:ScienceProtein InteractionsBiologyMultidisciplinaryMicroscopy ConfocalbiologyCell DeathCalpainCytochrome clcsh:RCytochromes cProteinsCalpainCysteine proteaseCell biologyMitochondriaProto-Oncogene Proteins c-bcl-2OncologyApoptosisbiology.proteinMedicinelcsh:QElectrophoresis Polyacrylamide GelGlobular ProteinsBCL2-related protein A1Research ArticlePloS one
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A Membrane-Bound Vertebrate Globin

2011

The family of vertebrate globins includes hemoglobin, myoglobin, and other O(2)-binding proteins of yet unclear functions. Among these, globin X is restricted to fish and amphibians. Zebrafish (Danio rerio) globin X is expressed at low levels in neurons of the central nervous system and appears to be associated with the sensory system. The protein harbors a unique N-terminal extension with putative N-myristoylation and S-palmitoylation sites, suggesting membrane-association. Intracellular localization and transport of globin X was studied in 3T3 cells employing green fluorescence protein fusion constructs. Both myristoylation and palmitoylation sites are required for correct targeting and m…

Protein StructureLipoylationGreen Fluorescent ProteinsMolecular Sequence Datalcsh:MedicineHemeBiochemistryCell membranechemistry.chemical_compoundModel OrganismsPalmitoylationhemic and lymphatic diseasesmedicineAnimalsRespiratory functionAmino Acid SequenceGlobinlcsh:ScienceProtein InteractionsBiologyZebrafishZebrafishMyristoylationHemoproteinsMultidisciplinarySequence Homology Amino Acidbiologylcsh:RCell MembraneMembrane ProteinsProteinsGene Expression Regulation DevelopmentalAnimal Modelsbiology.organism_classificationRecombinant ProteinsGlobinsGlobin foldOxygenmedicine.anatomical_structureBiochemistryMyoglobinchemistryImmunoglobulin GCytochemistrylcsh:QRabbitsResearch ArticleSubcellular FractionsPLoS ONE
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Unlocked Concanavalin A Forms Amyloid-like Fibrils from Coagulation of Long-lived "Crinkled'' Intermediates

2013

Understanding the early events during amyloid aggregation processes is crucial to single out the involved molecular mechanisms and for designing ad hoc strategies to prevent and reverse amyloidogenic disorders. Here, we show that, in conditions in which the protein is positively charged and its conformational flexibility is enhanced, Concanavalin A leads to fibril formation via a non-conventional aggregation pathway. Using a combination of light scattering, circular dichroism, small angle X-ray scattering, intrinsic (Tryptophan) and extrinsic (ANS) fluorescence and confocal and 2-photon fluorescence microscopy we characterize the aggregation process as a function of the temperature. We high…

Macromolecular AssembliesProteomicsCircular dichroismProtein StructureAmyloidProtein FoldingScienceMedical BiotechnologyBiophysics02 engineering and technologyFibrilBiochemistryProtein Chemistry03 medical and health sciencesProtein structureMedicinsk bioteknologiFluorescence microscopeNative stateConcanavalin ACoagulation (water treatment)Protein InteractionsBiology030304 developmental biology0303 health sciencesprotein aggregation amyloid concanavalin A intermediates spectroscopy advanced fluorescence microscopyMultidisciplinaryChemical PhysicsChemistryPhysicsCircular DichroismQRProteins021001 nanoscience & nanotechnologyProtein Structure TertiaryLuminescent ProteinsBiochemistryBiophysicsMedicineProtein folding0210 nano-technologyHydrophobic and Hydrophilic InteractionsFunction (biology)Research Article
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Editorial: Protein Interaction Networks in Health and Disease

2016

The identification and annotation of protein-protein interactions (PPIs) is of great importance in systems biology. Big data produced from experimental or computational approaches allow not only the construction of large protein interaction maps but also expand our knowledge on how proteins build up molecular complexes to perform sophisticated tasks inside a cell. However, if we want to accurately understand the functionality of these complexes, we need to go beyond the simple identification of PPIs. We need to know when and where an interaction happens in the cell and also understand the flow of information through a protein interaction network. Another perspective of the research on PPI n…

0301 basic medicineprotein networkdiseasePhysiologySystems biologyCellular homeostasissystems biologyComputational biologyprotein functionBiologyProteomicscomputer.software_genreprotein interactionsInteractomeProtein–protein interaction03 medical and health sciences030104 developmental biologyHuman interactomeInteraction networkGeneticsMolecular MedicineData miningcomputerGenetics (clinical)Biological networkFrontiers in Genetics
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Direct observation of alpha-lactalbumin, adsorption and incorporation into lipid membrane and formation of lipid/protein hybrid structures

2019

The interaction between proteins and membranes is of great interest in biomedical and biotechnological research for its implication in many functional and dysfunctional processes. We present an experimental study on the interaction between model membranes and alpha-lactalbumin (alpha-La). alpha-La is widely studied for both its biological function and its anti-tumoral properties. We use advanced fluorescence microscopy and spectroscopy techniques to characterize alpha-La-membrane mechanisms of interaction and alpha-La-induced modifications of membranes when insertion of partially disordered regions of protein chains in the lipid bilayer is favored. Moreover, using fluorescence lifetime imag…

0301 basic medicineFluorescence-lifetime imaging microscopyProtein ConformationLipid BilayersBiophysics02 engineering and technologyBiochemistryMembrane Lipids03 medical and health sciencesProtein structureMembrane fluidityFluorescence microscopeAnimalsHumansLipid bilayerMolecular BiologyFluorescent DyesChemistryMembrane structure021001 nanoscience & nanotechnologyLipids2-PHOTON FLUORESCENCE MICROSCOPY; MOLTEN GLOBULE STATE; PARTIALLY FOLDED CONFORMATIONS; PROTEIN INTERACTIONS; CIRCULAR-DICHROISM; AMPHITROPIC PROTEINS; AMYLOID AGGREGATION; PHASOR APPROACH; OLEIC-ACID; LAURDANSpectrometry Fluorescence030104 developmental biologyMembranefluorescence FLIM Protein membrane interaction IDPLactalbuminBiophysicsCattleAdsorption0210 nano-technologyProtein adsorptionBiochimica et Biophysica Acta (BBA) - General Subjects
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Human Hsp60 with Its Mitochondrial Import Signal Occurs in Solution as Heptamers and Tetradecamers Remarkably Stable over a Wide Range of Concentrati…

2014

It has been established that Hsp60 can accumulate in the cytosol in various pathological conditions, including cancer and chronic inflammatory diseases. Part or all of the cytosolic Hsp60 could be naive, namely, bear the mitochondrial import signal (MIS), but neither the structure nor the in solution oligomeric organization of this cytosolic molecule has still been elucidated. Here we present a detailed study of the structure and self-organization of naive cytosolic Hsp60 in solution. Results were obtained by different biophysical methods (light and X ray scattering, single molecule spectroscopy and hydrodynamics) that all together allowed us to assay a wide range of concentrations of Hsp60…

LightCancer Treatmentlcsh:MedicinePlasma protein bindingMitochondrionBiochemistrySmall-Angle ScatteringCell-free systemScatteringchemistry.chemical_compoundCytosolProtein structureBasic Cancer ResearchMacromolecular Structure AnalysisMedicine and Health SciencesScattering RadiationHsp60 Gro EL Recombinant proteinslcsh:ScienceAdenosine TriphosphatasesMultidisciplinaryAqueous solutionMolecular StructurePhysicsElectromagnetic RadiationHydrolysisRecombinant ProteinsMitochondriaChemistryMonomerOncologyBiochemistryPhysical SciencesInterdisciplinary PhysicsHSP60Research ArticleProtein BindingProtein Structureanimal structuresBiophysicschemical and pharmacologic phenomenaBiologycomplex mixturesMitochondrial ProteinsHumansProtein InteractionsMolecular BiologyInflammationChemical PhysicsCell-Free Systemlcsh:RfungiLight ScatteringBiology and Life SciencesProteinsProtein ComplexesChaperonin 60Chaperone ProteinsCytosolSpectrometry FluorescencechemistryMolecular Complexeslcsh:QPLoS ONE
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