Search results for "Shock proteins"

showing 10 items of 347 documents

Evolution of the leucine gene cluster in Buchnera aphidicola: insights from chromosomal versions of the cluster.

2004

ABSTRACT In Buchnera aphidicola strains associated with the aphid subfamilies Thelaxinae, Lachninae, Pterocommatinae, and Aphidinae, the four leucine genes ( leuA , - B , - C , and - D ) are located on a plasmid. However, these genes are located on the main chromosome in B. aphidicola strains associated with the subfamilies Pemphiginae and Chaitophorinae. The sequence of the chromosomal fragment containing the leucine cluster and flanking genes has different positions in the chromosome in B. aphidicola strains associated with three tribes of the subfamily Pemphiginae and one tribe of the subfamily Chaitophorinae. Due to the extreme gene order conservation of the B. aphidicola genomes, the v…

ChaitophorinaeSubfamilygenome sequenceGenetics and Molecular BiologyMicrobiologyGenomemolecular characterizationsymbiotic bacteriaPlasmidschizaphis-graminumBuchneraLeucinemitochondrial-dnaplasmidGene clusterMolecular BiologyGeneHeat-Shock ProteinsPhylogenyGeneticsRecombination GeneticBinding SitesbiologyEscherichia coli ProteinsChromosomeChromosomes Bacterialbiology.organism_classificationPRI Bioscienceaphidsendosymbiotic bacteriaMultigene Familyescherichia-coliBuchneraanthranilate synthase trpegPlasmidsJournal of bacteriology
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CtsR is the master regulator of stress response gene expression in Oenococcus oeni.

2005

ABSTRACT Although many stress response genes have been characterized in Oenococcus oeni , little is known about the regulation of stress response in this malolactic bacterium. The expression of eubacterial stress genes is controlled both positively and negatively at the transcriptional level. Overall, negative regulation of heat shock genes appears to be more widespread among gram-positive bacteria. We recently identified an ortholog of the ctsR gene in O. oeni . In Bacillus subtilis , CtsR negatively regulates expression of the clp genes, which belong to the class III family of heat shock genes. The ctsR gene of O. oeni is cotranscribed with the downstream clpC gene. Sequence analysis of t…

ChaperoninsOperonMolecular Sequence DataBiologyMicrobiologyGenome03 medical and health sciencesBacterial ProteinsSigma factorHeat shock proteinOperon[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyGene RegulationPromoter Regions GeneticMolecular BiologyGeneHeat-Shock Proteins030304 developmental biologyRegulator geneOenococcus oeniGeneticsRegulation of gene expressionAdenosine Triphosphatases0303 health sciencesBase Sequence030306 microbiologyCTSRGene Expression Regulation Bacterialbiology.organism_classificationDNA-Binding ProteinsGram-Positive CocciRepressor ProteinsMutagenesis Site-DirectedOenococcus oeniGenome BacterialHeat-Shock ResponseBacillus subtilisMolecular ChaperonesJournal of bacteriology
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Stress response in mesoangioblast stem cells

2006

Stem cells are presumed to survive various stresses, since they are recruited to areas of tissue damage and regeneration, where inflammatory cytokines and cytotoxic cells may result in severe cell injury. We explored the ability of mesoangioblasts to respond to different cell stresses such as heat, heavy metals and osmotic stress, by analyzing heat shock protein (HSP)70 synthesis as a stress indicator. We found that the A6 mesoangioblast stem cells constitutively synthesize HSP70 in a heat shock transcription factor (HSF)-independent way. However, A6 respond to heat shock and cadmium treatment by synthesizing HSP70 over the constitutive expression and this synthesis is HSF1 dependent. The e…

Chloramphenicol O-AcetyltransferaseHot TemperatureOsmotic shockRecombinant Fusion ProteinsBlotting WesternHypertonic SolutionsElectrophoretic Mobility Shift AssayBiologyResponse ElementsTransfectionMesodermMiceSTRESS RESPONSE STEM CELLS MOUSE MESOANGIOBLASTS.Heat Shock Transcription FactorsHeat shock proteinMetals HeavyAnimalsRNA MessengerHSF1Promoter Regions GeneticMolecular BiologyCells CulturedMesoangioblastHSC70 Heat-Shock ProteinsCell BiologyTransfectionHematopoietic Stem CellsMolecular biologyCell biologyHsp70Heat shock factorDNA-Binding ProteinsGene Expression RegulationStem cellTranscription Factors
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Endoplasmic reticulum‐resident chaperones modulate the inflammatory and angiogenic responses of endothelial cells

2015

SummaryBackground Wound healing depends on a well-balanced regulation of inflammation and angiogenesis. In chronic wounds the healing process is disturbed and inflammation persists. Regulation of wound closure is controlled by transmembrane and extracellular proteins, the folding and maturation of which occur in the endoplasmic reticulum (ER) by ER-resident chaperone machinery. Objectives To study the role of the ER-resident chaperones BiP/Grp78, its cochaperone Mdg1/ERdJ4, and Grp94 in chronic, nonhealing wounds. Methods Immunohistochemical staining of these chaperones in individual human biopsies and investigation of the possible role of BiP and Mdg1 in endothelial cells, focusing on thei…

Chronic woundChemokineAngiogenesisDown-RegulationNeovascularization PhysiologicInflammationDermatologyEndoplasmic ReticulumProinflammatory cytokinemedicineHumansEndoplasmic Reticulum Chaperone BiPCells CulturedHeat-Shock ProteinsInflammationWound HealingMembrane GlycoproteinsbiologyTumor Necrosis Factor-alphaEndoplasmic reticulumEndothelial CellsMembrane ProteinsHSP40 Heat-Shock ProteinsCell biologyChaperone (protein)Chronic Diseasebiology.proteinmedicine.symptomWound healingMolecular ChaperonesBritish Journal of Dermatology
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Mitochondrial compartment: a possible target of cadmium effects on breast epithelial cells.

2009

Cadmium–breast epithelial cell interactions were studied by analyzing some mitochondria-related aspects of stress response. We treated immortalized non-tumor breast cells with 5 or 50 μM CdCl2 for 24 or 96 h demonstrating that the exposure did not cause a significant mitochondrial proliferation, while it induced a significant increase in the respiratory activity and mitochondrial polarization. In addition, we found that hsp60 was up-regulated while hsp70 and COXII and COXIV were down-regulated. The mRNA for hsp70 remained constant and only the inducible form of the 70-kDa heat shock protein was over expressed. The mRNAs for COXII and COXIV remained constant after 24 h and increased after lo…

Clinical chemistryCadmium - Mitochondria - Stress - Breast EpithelialClinical BiochemistryCell RespirationMitochondrionBiologyCell LineElectron Transport Complex IVHeat shock proteinmedicineHumansHSP70 Heat-Shock ProteinsBreastCytotoxicityMolecular BiologyMembrane Potential MitochondrialMessenger RNAMembranesDose-Response Relationship DrugEpithelial CellsCell BiologyGeneral MedicineChaperonin 60EpitheliumCell biologyHsp70Mitochondriamedicine.anatomical_structureGene Expression RegulationHSP60FemaleCadmium
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Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 an…

2003

Nuclear domains called ND10 or PML bodies might function as nuclear depots by recruiting or releasing certain proteins. Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences. Exposure to sublethal environmental stress revealed a sequential release of ND10-associated proteins. Upon heat shock Daxx and Sp100 were released but PML remained, whereas exposure to subtoxic concentrations of CdCl2 induced the release of ND10-associated proteins, including PML, with Sp100 remaining in a few sites. In both cases,recovery times were simil…

Co-Repressor ProteinsMAP Kinase Signaling SystemMacromolecular SubstancesSUMO-1 ProteinPromyelocytic Leukemia ProteinMicePromyelocytic leukemia proteinDeath-associated protein 6Stress PhysiologicalHeat shock proteinEndopeptidasesAnimalsHSP70 Heat-Shock ProteinsEnzyme InhibitorsHeat shockTranscription factorCells CulturedHeat-Shock ProteinsbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsCell BiologyCell Nucleus StructuresNeoplasm ProteinsCell biologyHsp70Cysteine EndopeptidasesEukaryotic CellsGene Expression RegulationImmunologybiology.proteinSignal transductionCarrier ProteinsCo-Repressor ProteinsHeat-Shock ResponseCadmiumMolecular ChaperonesTranscription FactorsJournal of Cell Science
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Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.

2013

ATP regulates the function of many proteins in the cell by transducing its binding and hydrolysis energies into protein conformational changes by mechanisms which are challenging to identify at the atomic scale. Based on molecular dynamics (MD) simulations, a method is proposed to analyze the structural changes induced by ATP binding to a protein by computing the effective free-energy landscape (FEL) of a subset of its coordinates along its amino-acid sequence. The method is applied to characterize the mechanism by which the binding of ATP to the nucleotide-binding domain (NBD) of Hsp70 propagates a signal to its substrate-binding domain (SBD). Unbiased MD simulations were performed for Hsp…

Conformational changeProtein ConformationAllosteric regulationPlasma protein bindingMolecular Dynamics SimulationCellular and Molecular NeuroscienceProtein structureAdenosine TriphosphateGeneticsHSP70 Heat-Shock ProteinsMolecular Biologylcsh:QH301-705.5Nuclear Magnetic Resonance BiomolecularEcology Evolution Behavior and SystematicsEcologybiologyChemistryEscherichia coli ProteinsEnergy landscapeComputational Theory and MathematicsBiochemistrylcsh:Biology (General)Docking (molecular)Modeling and SimulationChaperone (protein)Biophysicsbiology.proteinBinding domainProtein BindingResearch ArticlePLoS computational biology
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Multivariate analysis in the identification of biological targets for designed molecular structures: The BIOTA protocol

2013

In this work the new protocol BIOlogical Target Assignation (BIOTA) for the prediction of the biological target from molecular structures is proposed. BIOTA is based on the Principal Components Analysis (PCA) application on a matrix of ligands versus molecular descriptors. The application of BIOTA could allow to hypothesize the mechanism of action of a candidate drug prior to its biological evaluation or to repurpose old drugs. The protocol can be fine-tuned by choosing opportune targets (biological or not) and molecular descriptors, and it can be useful in every fields in with it is possible to collect set of compounds with known properties. The robustness of the protocol depends from diff…

CorrectnessComputational biologyBiologyBioinformaticsMolecular descriptorDrug DiscoveryHumansHSP90 Heat-Shock ProteinsMolecular Targeted TherapyPharmacologyPrincipal Component AnalysisBiological dataintegumentary systemBIOTA protocol Biological target Inhibitors PCA Drugs repurposingfungiOrganic ChemistryDrug RepositioningRobustness (evolution)BiotaGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaBiological targetSettore CHIM/03 - Chimica Generale E InorganicaMultivariate AnalysisPrincipal component analysisIdentification (biology)
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Vipp1: a very important protein in plastids?!

2011

As a key feature in oxygenic photosynthesis, thylakoid membranes play an essential role in the physiology of plants, algae, and cyanobacteria. Despite their importance in the process of oxygenic photosynthesis, their biogenesis has remained a mystery to the present day. A decade ago, vesicle-inducing protein in plastids 1 (Vipp1) was described to be involved in thylakoid membrane formation in chloroplasts and cyanobacteria. Most follow-up studies clearly linked Vipp1 to membranes and Vipp1 interactions as well as the defects observed after Vipp1 depletion in chloroplasts and cyanobacteria indicate that Vipp1 directly binds to membranes, locally stabilizes bilayer structures, and thereby ret…

CyanobacteriaChloroplastsPhysiologyMembrane Proteinsfood and beveragesBiological TransportPlant ScienceBiologyCyanobacteriabiology.organism_classificationPhotosynthesisThylakoidsCell biologyChloroplastMembraneBacterial ProteinsThylakoidPlastidsPlastidPhage shockHeat-Shock ProteinsBiogenesisSignal TransductionJournal of Experimental Botany
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Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

2004

ABSTRACT Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 …

Cytoplasmanimal structuresImmunoprecipitationvirusesImmunologyActive Transport Cell Nucleusmacromolecular substancesBiologyMicrobiologyVirusGreen fluorescent proteinCell Line TumorVirologyAnimalsHSP70 Heat-Shock ProteinsCOS cellsHSC70 Heat-Shock ProteinsVirionOncogene Proteins ViralMolecular biologyVirus-Cell InteractionsTransport proteinCell biologyProtein TransportCapsidCytoplasmInsect ScienceChaperone (protein)COS Cellsembryonic structuresbiology.proteinCapsid ProteinsJournal of Virology
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