Search results for "Fluorescence Recovery after Photobleaching"

showing 10 items of 21 documents

Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
researchProduct

Distribution and Dynamics of Transcription-Associated Proteins during Parvovirus Infection

2012

ABSTRACT Canine parvovirus (CPV) infection leads to reorganization of nuclear proteinaceous subcompartments. Our studies showed that virus infection causes a time-dependent increase in the amount of viral nonstructural protein NS1 mRNA. Fluorescence recovery after photobleaching showed that the recovery kinetics of nuclear transcription-associated proteins, TATA binding protein (TBP), transcription factor IIB (TFIIB), and poly(A) binding protein nuclear 1 (PABPN1) were different in infected and noninfected cells, pointing to virus-induced alterations in binding dynamics of these proteins.

Parvovirus CanineViral nonstructural proteinvirusesImmunologyMicrobiologyParvoviridae Infections03 medical and health sciencesVirologyAnimalsTranscription factor030304 developmental biology0303 health sciencesbiologyParvovirusBinding protein030302 biochemistry & molecular biologyCanine parvovirusFluorescence recovery after photobleachingbiology.organism_classificationMolecular biology3. Good healthVirus-Cell InteractionsCell CompartmentationInsect Sciencebiology.proteinTATA-binding proteinTranscription factor II BSubcellular FractionsTranscription Factors
researchProduct

Parvovirus induced alterations in nuclear architecture and dynamics.

2009

The nucleus of interphase eukaryotic cell is a highly compartmentalized structure containing the three-dimensional network of chromatin and numerous proteinaceous subcompartments. DNA viruses induce profound changes in the intranuclear structures of their host cells. We are applying a combination of confocal imaging including photobleaching microscopy and computational methods to analyze the modifications of nuclear architecture and dynamics in parvovirus infected cells. Upon canine parvovirus infection, expansion of the viral replication compartment is accompanied by chromatin marginalization to the vicinity of the nuclear membrane. Dextran microinjection and fluorescence recovery after ph…

Parvovirus CaninevirusesGreen Fluorescent Proteinslcsh:MedicineGenome ViralKidneyParvoviridae InfectionsParvovirus03 medical and health sciencesLääketieteen bioteknologia - Medical biotechnologymedicineAnimalsHumansNuclear membraneMolecular Biology/Chromatin Structurelcsh:Science030304 developmental biologyMolecular Biology/DNA ReplicationCell Nucleus0303 health sciencesMultidisciplinaryMicroscopy ConfocalbiologyParvoviruslcsh:R030302 biochemistry & molecular biologyDNA replicationFluorescence recovery after photobleachingDextransbiology.organism_classificationMolecular biologyChromatin3. Good healthChromatinCell biologyCell nucleusmedicine.anatomical_structureViral replicationVirology/Viral Replication and Gene RegulationCatslcsh:QCell Biology/Nuclear Structure and FunctionViral genome replicationFluorescence Recovery After PhotobleachingHeLa CellsResearch ArticlePloS one
researchProduct

Modification of Plasma Membrane Organization in Tobacco Cells Elicited by Cryptogein

2014

Abstract Lipid mixtures within artificial membranes undergo a separation into liquid-disordered and liquid-ordered phases. However, the existence of this segregation into microscopic liquid-ordered phases has been difficult to prove in living cells, and the precise organization of the plasma membrane into such phases has not been elucidated in plant cells. We developed a multispectral confocal microscopy approach to generate ratiometric images of the plasma membrane surface of Bright Yellow 2 tobacco (Nicotiana tabacum) suspension cells labeled with an environment sensitive fluorescent probe. This allowed the in vivo characterization of the global level of order of this membrane, by which w…

Physiology[SDV]Life Sciences [q-bio]BiophysicsContext (language use)Pyridinium CompoundsPlant ScienceBiologyArticleFungal ProteinsTobaccoGeneticsMembrane fluidity[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyFluorescent DyesPlasma membrane organizationChromatographyMicroscopy ConfocalPhotobleachingCell MembraneFluorescence recovery after photobleachingMembrane raftfood and beveragesPlant cellElicitorSterolsMembrane[SDE]Environmental SciencesBiophysicsFlagellinSignal Transduction
researchProduct

Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
researchProduct

Desmosomes: interconnected calcium-dependent structures of remarkable stability with significant integral membrane protein turnover

2002

Desmosomes are prominent cell adhesion structures that are major stabilizing elements, together with the attached cytoskeletal intermediate filament network, of the cytokeratin type in epithelial tissues. To examine desmosome dynamics in tightly coupled cells and in situations of decreased adhesion, fluorescent desmosomal cadherin desmocollin 2a (Dsc2a) chimeras were stably expressed in human hepatocellular carcinoma-derived PLC cells (clone PDc-13) and in Madin-Darby canine kidney cells (clone MDc-2) for the continuous monitoring of desmosomes in living cells. The hybrid polypeptides integrated specifically and without disturbance into normal-appearing desmosomes that occurred in associati…

Time FactorsRecombinant Fusion ProteinsBiologyCell LineCytokeratinDogsGenes ReporterDesmosomeCell AdhesionmedicineAnimalsHumansDesmosomal CadherinsCell adhesionIntermediate filamentCytoskeletonDesmocollinsMembrane GlycoproteinsCadherinCarcinomaCell CycleLiver NeoplasmsFluorescence recovery after photobleachingEpithelial CellsDesmosomesCell BiologyCell biologyMicroscopy Electronmedicine.anatomical_structureMicroscopy FluorescenceKeratinsCalciumJournal of Cell Science
researchProduct

Polar Localization of a Tripartite Complex of the Two-Component System DcuS/DcuR and the Transporter DctA in Escherichia coli Depends on the Sensor K…

2014

The C4-dicarboxylate responsive sensor kinase DcuS of the DcuS/DcuR two-component system of E. coli is membrane-bound and reveals a polar localization. DcuS uses the C4-dicarboxylate transporter DctA as a co-regulator forming DctA/DcuS sensor units. Here it is shown by fluorescence microscopy with fusion proteins that DcuS has a dynamic and preferential polar localization, even at very low expression levels. Single assemblies of DcuS had high mobility in fast time lapse acquisitions, and fast recovery in FRAP experiments, excluding polar accumulation due to aggregation. DctA and DcuR fused to derivatives of the YFP protein are dispersed in the membrane or in the cytosol, respectively, when …

Yellow fluorescent proteinCardiolipinslcsh:MedicineMicrobiologyMreBMicrobial PhysiologyBacterial Physiologylcsh:ScienceCytoskeletonMicrobial MetabolismDicarboxylic Acid TransportersMultidisciplinaryEscherichia coli K12biologyBacterial GrowthEscherichia coli Proteinslcsh:RMicrobial Growth and DevelopmentBiology and Life SciencesFluorescence recovery after photobleachingBacteriologyFusion proteinTwo-component regulatory systemBacterial BiochemistryTransport proteinDNA-Binding ProteinsProtein TransportBiochemistryCytoplasmMultiprotein ComplexesBiophysicsbiology.proteinlcsh:QProtein KinasesResearch ArticleDevelopmental BiologyTranscription FactorsPLoS ONE
researchProduct

Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1.

2015

AbstractBacteriophage PRD1, which has been studied intensively at the structural and functional levels, still has some gene products with unknown functions and certain aspects of the PRD1 assembly process have remained unsolved. In this study, we demonstrate that the phage-encoded non-structural proteins P17 and P33, either individually or together, complement the defect in a temperature-sensitive GroES mutant of Escherichia coli for host growth and PRD1 propagation. Confocal microscopy of fluorescent fusion proteins revealed co-localisation between P33 and P17 as well as between P33 and the host chaperonin GroEL. A fluorescence recovery after photobleaching assay demonstrated that the diff…

assemblychaperoninvirusesMutantfluorescence recovery after photobleachingViral Nonstructural Proteinsmedicine.disease_causeVirus ReplicationChaperoninHost-Parasite InteractionsBacteriophagebacteriophageVirologymedicineEscherichia colifluorescent proteinBacteriophage PRD1Escherichia colimembrane virusMicroscopy Confocalbiologyprotein localisationVirus Assemblyta1182Fluorescence recovery after photobleachingGroESChaperonin 60biology.organism_classificationFusion proteinGroEL3. Good healthCell biologyVirology
researchProduct

Identification of Novel Principles of Keratin Filament Network Turnover in Living Cells

2004

It is generally assumed that turnover of the keratin filament system occurs by exchange of subunits along its entire length throughout the cytoplasm. We now present evidence that a circumscribed submembranous compartment is actually the main site for network replenishment. This conclusion is based on the following observations in living cells synthesizing fluorescent keratin polypeptides: 1) Small keratin granules originate in close proximity to the plasma membrane and move toward the cell center in a continuous motion while elongating into flexible rod-like fragments that fuse with each other and integrate into the peripheral KF network. 2) Recurrence of fluorescence after photobleaching i…

chemistry.chemical_classificationKeratin Filamentintegumentary systemFluorescence recovery after photobleachingArticlesmacromolecular substancesCell BiologyBiologyCell biologychemistryCytoplasmKeratinCell cortexIntermediate filamentCytoskeletonMolecular BiologyMitosisMolecular Biology of the Cell
researchProduct

Dominance of Chain Entanglement over Transient Sticking on Chain Dynamics in Hydrogen-Bonded Supramolecular Polymer Networks in the Melt

2018

The chain dynamics in supramolecular polymer networks is determined by the interplay of the kinetics of transient interchain association and relaxation of the network chains themselves. This interplay can be addressed by studying model supramolecular polymer networks in which the number of associative side groups and the molar mass of the covalently jointed backbone polymers are both varied systematically. To realize this idea, we use precursor chains with three different molar masses, which comes along with different extents of entanglement in the melt state. For each molar mass, the precursor polymers are functionalized with three different relative contents of associative side groups, gi…

chemistry.chemical_classificationMolar massMaterials sciencePolymers and PlasticsOrganic ChemistryKineticsFluorescence recovery after photobleaching02 engineering and technologyQuantum entanglementPolymer010402 general chemistry021001 nanoscience & nanotechnologyThermal diffusivity01 natural sciences0104 chemical sciencesInorganic ChemistrySupramolecular polymerschemistryChemical physicsCovalent bondMaterials Chemistry0210 nano-technologyMacromolecules
researchProduct