Search results for "Protein S"

showing 10 items of 1431 documents

The Greenland shark Somniosus microcephalus—Hemoglobins and ligand-binding properties

2017

A large amount of data is currently available on the adaptive mechanisms of polar bony fish hemoglobins, but structural information on those of cartilaginous species is scarce. This study presents the first characterisation of the hemoglobin system of one of the longest-living vertebrate species (392 +/- 120 years), the Arctic shark Somniosus microcephalus. Three major hemoglobins are found in its red blood cells and are made of two copies of the same a globin combined with two copies of three very similar beta subunits. The three hemoglobins show very similar oxygenation and carbonylation properties, which are unaffected by urea, a very important compound in marine elasmobranch physiology.…

---0301 basic medicinegenetic structuresProtein ConformationGreenlandlcsh:MedicineRESONANCE RAMAN-SPECTRAHETERODONTUS-PORTUSJACKSONISpectrum Analysis RamanBiochemistrychemistry.chemical_compoundHemoglobinsProtein structureAMINO-ACID SEQUENCEAnimal CellsSequence Analysis ProteinRed Blood CellsUreaNOTOTHENIOID FISHESPost-Translational Modificationlcsh:ScienceHemeChondrichthyesMultidisciplinarybiologyChemistryOrganic CompoundsChemical ReactionsVertebrateEukaryotaMOLECULAR ADAPTATIONSMicrocephalusGlobinsChemistryBiochemistryOptical EquipmentVertebratesPhysical SciencesEngineering and TechnologyCellular TypesResearch ArticleEnvironmental MonitoringProtein BindingQUATERNARY STRUCTURESAllosteric regulationEquipmentSTRETCHING FREQUENCIESHeme03 medical and health sciencesOXYGEN-BINDINGbiology.animalAnimals14. Life underwaterGlobinHemoglobinPhotolysisBlood Cells030102 biochemistry & molecular biologyLaserslcsh:ROrganic ChemistryOrganismsChemical CompoundsBiology and Life SciencesProteinsxxxCell Biologybiology.organism_classificationCARTILAGINOUS FISHOxygen030104 developmental biologySomniosusFishSharkslcsh:QHemoglobinProtein MultimerizationELASMOBRANCH HEMOGLOBINElasmobranchiiPLoS ONE
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MD Simulation Investigation on the Binding Process of Smoke-Derived Germination Stimulants to Its Receptor

2019

Karrikins (KARs) are a class of smoke-derived seed germination stimulants with great significance in both agriculture and plant biology. By means of direct binding to the receptor protein KAI2, the compounds can initiate the KAR signal transduction pathway, hence triggering germination of the dormant seeds in the soil. In the research, several molecular dynamics (MD) simulation techniques were properly integrated to investigate the binding process of KAR1 to KAI2 and reveal the details of the whole binding event. The calculated binding free energy, -7.00 kcal/mol, is in good agreement with the experimental measurement, -6.83 kcal/mol. The obtained PMF profile indicates the existence of thre…

010304 chemical physicsProtein ConformationChemistryGeneral Chemical EngineeringGerminationGeneral ChemistryPlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesLigand (biochemistry)01 natural sciences0104 chemical sciencesComputer Science Applications010404 medicinal & biomolecular chemistryMolecular dynamicsProtein structure0103 physical sciencesMoleBiophysicsThermodynamicsMoleculeSignal transductionReceptorPlant ProteinsProtein BindingJournal of Chemical Information and Modeling
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cDNA sequences of two arylphorin subunits of an insect biliprotein: phylogenetic differences and gene duplications during evolution of hexamerins-imp…

2016

Arylphorins represent a conserved class of hexameric ∼500 kDa insect hemolymph glycoproteins, rich in aromatic amino acids, which are produced in large quantities at the larval stage as reserves for metamorphosis and egg development. The recently isolated arylphorin from the moth Cerura vinula is unique in being complexed to a novel farnesylated bilin. Protein sequencing suggested the presence of two different ∼85 kDa subunits. Here, we report the complete coding sequences of two cDNAs encoding two arylphorins subunits with 67% identity and calculated physicochemical characteristics in agreement with the isolated holoprotein. Our phylogenetic analyses of the hexamerins revealed monophyletic…

0106 biological sciences0301 basic medicineGeneticsPhylogenetic treebiologyCerura vinulaProtein subunitAntheraea pernyibiology.organism_classification01 natural sciences010602 entomology03 medical and health sciences030104 developmental biologyProtein sequencingPhylogeneticsComplementary DNAGeneticsMolecular MedicineAnimal Science and ZoologyPeptide sequenceEcology Evolution Behavior and SystematicsDevelopmental BiologyJournal of Experimental Zoology Part B: Molecular and Developmental Evolution
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The chaperone-like protein Cdc48 regulates ubiquitin-proteasome system in plants.

2021

The degradation of misfolded proteins is mainly mediated by the ubiquitin-proteasome system (UPS). UPS can be assisted by the protein Cdc48 but the relationship between UPS and Cdc48 in plants has been poorly investigated. Here, we analyzed the regulation of UPS by Cdc48 in tobacco thanks to two independent cell lines overexpressing Cdc48 constitutively and plant leaves overexpressing Cdc48 transiently. In the cell lines, the accumulation of ubiquitinated proteins was affected both quantitatively and qualitatively and the amount of proteasomal subunits was modified, while proteolytic activities were unchanged. Similarly, the over-expression of Cdc48 in planta impacted the accumulation of ub…

0106 biological sciences0301 basic medicineHypersensitive responseProgrammed cell deathProteasome Endopeptidase ComplexPhysiologyProtein subunitubiquitinomePlant Science01 natural sciencescryptogeinCdc48Fungal Proteins03 medical and health sciences[CHIM.ANAL]Chemical Sciences/Analytical chemistryValosin Containing ProteinTobacco[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyPlant ImmunityPlant ProteinsbiologyChemistryUbiquitinUbiquitin homeostasisPlants Genetically ModifiedUbiquitinated ProteinsElicitorCell biology030104 developmental biologyproteasomeProteasomeCell cultureChaperone (protein)biology.protein010606 plant biology & botanyPlant, cellenvironmentREFERENCES
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Jumping on the Edge—First Evidence for a 2 × 6-meric Hemocyanin in Springtails

2019

Hemocyanins are respiratory dioxygen carrier proteins found in many arthropods including ancient terrestrial species such as spiders and scorpions as well as marine horseshoe crabs. As hemocyanins are highly conserved in this lineage, it is possible to observe an evolutionary descent through its subunits and their overall structure. Unfortunately, little is known about the structure and function of hexapod hemocyanins. Using recent springtail taxa (Collembola) as models for basal hexapods, and the help of electron microscopy, light scattering, SDS PAGE, and Western blot, we could demonstrate for the first time the presence of 2 × 6-meric hemocyanins in the hemolymph of hexapods. The quatern…

0106 biological sciences0301 basic medicineLineage (evolution)medicine.medical_treatmentlcsh:QR1-502Zoologychemical and pharmacologic phenomenaSpringtail010603 evolutionary biology01 natural sciencesBiochemistrycomplex mixtureslcsh:MicrobiologyArthropod Proteins03 medical and health sciencesCrustaceaHemolymphmedicineterrestrializationAnimalsProtein Structure QuaternaryMolecular BiologyArthropodsbiologyspringtailsCommunicationHemocyaninbiology.organism_classificationhexapodsCrustaceanHorseshoe crabRespiratory protein030104 developmental biologyHemocyaninsCollembolaProtein quaternary structurehemocyaninProtein MultimerizationBiomolecules
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Sorting Motifs Involved in the Trafficking and Localization of the PIN1 Auxin Efflux Carrier

2016

In contrast with the wealth of recent reports about the function of μ-adaptins and clathrin adaptor protein (AP) complexes, there is very little information about the motifs that determine the sorting of membrane proteins within clathrin-coated vesicles in plants. Here, we investigated putative sorting signals in the large cytosolic loop of the Arabidopsis (Arabidopsis thaliana) PIN-FORMED1 (PIN1) auxin transporter, which are involved in binding μ-adaptins and thus in PIN1 trafficking and localization. We found that Phe-165 and Tyr-280, Tyr-328, and Tyr-394 are involved in the binding of different μ-adaptins in vitro. However, only Phe-165, which binds μA(μ2)- and μD(μ3)-adaptin, was found …

0106 biological sciences0301 basic medicinePhysiologyPhenylalanineGreen Fluorescent ProteinsMutantArabidopsisPlant ScienceProtein Sorting SignalsEndoplasmic ReticulumEndocytosis01 natural sciencesClathrin03 medical and health sciencesCytosolGeneticsGuanine Nucleotide Exchange FactorsSecretory pathwaybiologyArabidopsis ProteinsEndoplasmic reticulumMembrane Transport ProteinsSignal transducing adaptor proteinArticlesPlants Genetically ModifiedClathrinEndocytosisAdaptor Protein Complex mu SubunitsTransport proteinCell biologyProtein Transport030104 developmental biologyProtein Sorting SignalsMutationbiology.protein010606 plant biology & botanyPlant Physiology
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Loss of

2020

The early secretory pathway involves bidirectional transport between the endoplasmic reticulum (ER) and the Golgi apparatus and is mediated by coat protein complex I (COPI)-coated and coat protein complex II (COPII)-coated vesicles. COPII vesicles are involved in ER to Golgi transport meanwhile COPI vesicles mediate intra-Golgi transport and retrograde transport from the Golgi apparatus to the ER. The key component of COPI vesicles is the coatomer complex, that is composed of seven subunits (α/β/β'/γ/δ/ε/ζ). In Arabidopsis two genes coding for the β-COP subunit have been identified, which are the result of recent tandem duplication. Here we have used a loss-of-function approach to study the…

0106 biological sciences0301 basic medicineProtein subunitArabidopsisPlant Sciencelcsh:Plant culture01 natural sciences03 medical and health sciencessymbols.namesakelcsh:SB1-1110coat protein II (COPII)Plantes Cèl·lules i teixitsCOPIICreixement (Plantes)Secretory pathwayOriginal Researchsalt stressChemistryEndoplasmic reticulumVesiclecoat protein I (COPI)plant growthCOPIGolgi apparatusCell biology030104 developmental biologyCoatomerβ-COPGolgi apparatussymbols010606 plant biology & botanyFrontiers in plant science
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ß-COP mutants show specific high sensitivity to chloride ions.

2021

Coat Protein I (COPI) consists of a complex (coatomer) formed by seven subunits (α-, β-, β’-, γ-, δ-, ε-, and ζ-COP) that is recruited to Golgi membranes to form vesicles that shuttle from the Golgi apparatus to the ER and between Golgi stacks. Recently, it has been described that loss of function mutants of the two Arabidopsis β-COP genes, β1-COP and β2-COP, showed increased sensitivity to salt stress (NaCl). Using a mixture of either Na(+) or Cl(−) salts, we have now found that β-COP mutants are specifically and highly sensitive to chloride ions.

0106 biological sciences0301 basic medicineShort CommunicationMutantArabidopsisSalt (chemistry)Plant ScienceBiology01 natural sciencesChlorideCoatomer Protein03 medical and health sciencessymbols.namesakeChloridesArabidopsismedicinechemistry.chemical_classificationIonsVesicleCOPIGolgi apparatusbiology.organism_classificationhumanitiesProtein Subunits030104 developmental biologyPhenotypechemistryCoatomerMutationsymbolsBiophysics010606 plant biology & botanymedicine.drugProtein BindingPlant signalingbehavior
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Enhancing heterologous protein expression and secretion in HEK293 cells by means of combination of CMV promoter and IFNα2 signal peptide

2016

Efficient production and secretion of recombinant proteins in mammalian cell lines relies in a combination of genetic, metabolic and culture strategy factors. The present work assesses the influence of two key genetic components of expression vectors (promoter and signal peptide) on protein production and secretion effciency in HEK293 cells expressing eGFP as a reporter protein. Firstly, the strength of 3 different promoters was evaluated using transient expression methods. Flow cytometry analysis revealed that the highest level of intracellular protein expression was found when eGFP was under the control of CMV promoter, being 3-times higher in comparison to the rest of the promoters teste…

0106 biological sciences0301 basic medicineSignal peptideGreen Fluorescent ProteinsCytomegalovirusHeterologousBioengineeringProtein Sorting SignalsBiology01 natural sciencesApplied Microbiology and BiotechnologyGreen fluorescent protein03 medical and health sciences010608 biotechnologyProtein biosynthesisHumansSecretionPromoter Regions GeneticExpression vectorInterferon-alphaPromoterGeneral MedicineMolecular biologyRecombinant ProteinsHEK293 Cells030104 developmental biologyCell cultureBiotechnologyJournal of Biotechnology
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Rigid Core and Flexible Terminus

2012

The structure of the major light-harvesting chlorophyll a/b complex (LHCII) was analyzed by pulsed EPR measurements and compared with the crystal structure. Site-specific spin labeling of the recombinant protein allowed the measurement of distance distributions over several intra- and intermolecular distances in monomeric and trimeric LHCII, yielding information on the protein structure and its local flexibility. A spin label rotamer library based on a molecular dynamics simulation was used to take the local mobility of spin labels into account. The core of LHCII in solution adopts a structure very similar or identical to the one seen in crystallized LHCII trimers with little motional freed…

0106 biological sciences0303 health sciencesPulsed EPRChemistryProtein dynamicsCell BiologySite-directed spin labeling01 natural sciencesBiochemistrylaw.invention03 medical and health sciencesB vitaminsCrystallographyProtein structurelawHelixElectron paramagnetic resonanceSpin labelMolecular Biology030304 developmental biology010606 plant biology & botanyJournal of Biological Chemistry
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