Search results for "Protein S"

showing 10 items of 1431 documents

Characterization of MRNP34, a novel methionine-rich nacre protein from the pearl oysters

2012

9 pages; International audience; Nacre of the Pinctada pearl oyster shells is composed of 98% CaCO(3) and 2% organic matrix. The relationship between the organic matrix and the mechanism of nacre formation currently constitutes the main focus regarding the biomineralization process. In this study, we isolated a new nacre matrix protein in P. margaritifera and P. maxima, we called Pmarg- and Pmax-MRNP34 (methionine-rich nacre protein). MRNP34 is a secreted hydrophobic protein, which is remarkably rich in methionine, and which is specifically localised in mineralizing the epithelium cells of the mantle and in the nacre matrix. The structure of this protein is drastically different from those …

0106 biological sciencesBiomineralizationCalcifying mantleMethionine-richMolecular Sequence DataClinical BiochemistryGene ExpressionBiologyMatrix (biology)engineering.materialProteomics010603 evolutionary biology01 natural sciencesBiochemistryLow complexity03 medical and health sciencesPaleontologychemistry.chemical_compoundCalcification PhysiologicMethionineAnimalsAmino Acid SequencePinctada[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsNacre030304 developmental biology0303 health sciencesMethionineViral matrix proteinOrganic ChemistryProteinsEpithelial Cells[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialsbiology.organism_classificationProtein Structure TertiarychemistryBiochemistryengineeringMolluscMatrix proteinPearlBiomineralizationPinctada
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SHAPE MATTERS: EFFECT OF POINT MUTATIONS ON RNA SECONDARY STRUCTURE

2013

A suitable model to dive into the properties of genotype-phenotype landscapes is the relationship between RNA sequences and their corresponding minimum free energy secondary structures. Relevant issues related to molecular evolvability and robustness to mutations have been studied in this framework. Here, we analyze the one-mutant neighborhood of the predicted secondary structure of 46 different RNAs, including tRNAs, viroids, larger molecules such as Hepatitis-δ virus, and several random sequences. The probability distribution of the effect of point mutations in linear structural motifs of the secondary structure is well fit by Pareto or Lognormal probability distributions functions, indep…

0106 biological sciencesGenetics0303 health sciencesPoint mutationRNARobustness (evolution)Computational biologyBiology010603 evolutionary biology01 natural sciencesNucleic acid secondary structureEvolvability03 medical and health sciencesControl and Systems EngineeringProbability distributionStructural motifRNA secondary structure sequence-structure map mutational effects linear motifsProtein secondary structure030304 developmental biologyAdvances in Complex Systems
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Bridging the Knowledge Gap for the Impact of Non-Thermal Processing on Proteins and Amino Acids

2019

Proteins represent one of the major food components that contribute to a wide range of biophysical functions and dictate the nutritional, sensorial, and shelf-life of food products. Different non-thermal processing technologies (e.g., irradiation, ultrasound, cold plasma, pulsed electric field, and high-pressure treatments) can affect the structure of proteins, and thus their solubility as well as their functional properties. The exposure of hydrophobic groups, unfolding followed by aggregation at high non-thermal treatment intensities, and the formation of new bonds have been reported to promote the modification of structural and functional properties of proteins. Several studies reported …

0106 biological sciencesHealth (social science)ReviewPlant Sciencecold plasmalcsh:Chemical technologyFree amino01 natural sciencesHealth Professions (miscellaneous)MicrobiologyPascalization0404 agricultural biotechnologyProtein structure010608 biotechnologylcsh:TP1-1185Food componentsSolubilityhigh-pressure processing2. Zero hungerchemistry.chemical_classificationultrasound04 agricultural and veterinary sciences040401 food scienceAmino acidpulsed electric fieldschemistryproteins and amino acidsFood productsBiophysicsIrradiationFood ScienceFoods
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Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: towards the characterization of "plant defense prote…

2003

Plants have evolved efficient mechanisms to resist pathogens. The earliest defense response is the hypersensitive response (HR) considered as the main step leading to plant systemic acquired resistance (SAR) that protects the whole plant against a large spectrum of pathogens. We showed previously that elicitation of defense reactions in tobacco cells by cryptogein, a proteinaceous elicitor of plant defense reactions, leads to a rapid and differential accumulation of transcripts corresponding to genes encoding defense-induced (din) subunits of 20S proteasome: beta1din, alpha3din and alpha6din.Here, expression of these three subunits was investigated by Northern blotting and by Western blotti…

0106 biological sciencesHypersensitive responseProteasome Endopeptidase Complex[SDV]Life Sciences [q-bio]Protein subunitBlotting WesternGene ExpressionBiology01 natural sciencesBiochemistryMixed Function OxygenasesFungal Proteins03 medical and health sciencesMultienzyme ComplexesTobaccoPlant defense against herbivoryElectrophoresis Gel Two-DimensionalNorthern blotComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesAlgal ProteinsProteinsCell BiologyBlotting NorthernMolecular biologyCell biologyElicitor[SDV] Life Sciences [q-bio]BlotPlant LeavesTobacco Mosaic VirusCysteine EndopeptidasesProteasomeEnzyme InductionREPONSE DE LA PLANTESystemic acquired resistance010606 plant biology & botanyPeptide HydrolasesThe international journal of biochemistrycell biology
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Nucleotide Variability at the Acetyl Coenzyme A Carboxylase Gene and the Signature of Herbicide Selection in the Grass Weed Alopecurus myosuroides (H…

2004

Acetyl coenzyme A carboxylase (ACCase) is the target of highly effective herbicides. We investigated the nucleotide variability of the ACCase gene in a sample of 18 black-grass (Alopecurus myosuroides [Huds.]) populations to search for the signature of herbicide selection. Sequencing 3,396 bp encompassing ACCase herbicide-binding domain in 86 individuals revealed 92 polymorphisms, which formed 72 haplotypes. The ratio of nonsynonymous versus synonymous substitutions was very low, in agreement with ACCase being a vital metabolic enzyme. Within black grass, most nonsynonymous substitutions were related to resistance to ACCase-inhibiting herbicides. Differentiation between populations was stro…

0106 biological sciencesNonsynonymous substitutionMolecular Sequence DataStatistics as TopicBiologyGenes PlantPoaceae01 natural sciencesLinkage DisequilibriumNucleotide diversity03 medical and health sciences[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyGeneticsVULPIN[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular BiologyGeneAllelesPhylogenyComputingMilieux_MISCELLANEOUSEcology Evolution Behavior and SystematicsSelection (genetic algorithm)030304 developmental biologychemistry.chemical_classificationGenetics0303 health sciencesPolymorphism GeneticBase SequenceModels GeneticHaplotypeAlopecurus myosuroidesGenetic VariationDNASequence Analysis DNAPesticidebiology.organism_classificationProtein Structure TertiaryEnzymeHaplotypeschemistrySoftwareAcetyl-CoA Carboxylase010606 plant biology & botanyMolecular Biology and Evolution
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Collisional mechanism of ligand release by Bombyx mori JHBP, a member of the TULIP / Takeout family of lipid transporters.

2020

International audience; Juvenile hormones (JHs) regulate important processes in insects, such as postembryonic development and reproduction. In the hemolymph of Lepidoptera, these lipophilic sesquiterpenic hormones are transported from their site of synthesis to target tissues by high affinity carriers, the juvenile hormone binding proteins (JHBPs). Lepidopteran JHBPs belong to a recently uncovered, yet very ancient family of proteins sharing a common lipid fold (TULIP domain) and involved in shuttling various lipid ligands. One important, but poorly understood aspect of JHs action, is the mechanism of hormone transfer to or through the plasma membranes of target cells. Since many membrane-…

0106 biological sciencesPhospholipidMothsLigands01 natural sciencesBiochemistryManduca sexta03 medical and health scienceschemistry.chemical_compoundProtein structureBombyx moriAnimalsMolecular Biology030304 developmental biology0303 health sciencesJHBPbiologyLigandTakeout-like proteinsfungiBombyx moriJuvenile HormoneIsothermal titration calorimetryBiological Transportbiology.organism_classificationBombyxLipid MetabolismTULIP domain010602 entomologyMembraneBiochemistrychemistryManduca sextaInsect ScienceJuvenile hormone[SDE]Environmental SciencesInsect ProteinsCarrier Proteins
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The Tonoplast H+ -ATPase of Acer pseudoplatanus is a vacuolar-type ATPase that operates with a phosphoenzyme intermediate

1995

The tonoplast H+-ATPase of Acer pseudoplatanus has been purified from isolated vacuoles. After solubilization, the purification procedure included size-exclusion and ion-exchange chromatography. The H+-ATPase consists of at least eight subunits, of 95, 66, 56, 54, 40, 38, 31, and 16 kD, that did not cross-react with polyclonal antibodies raised to the plasmalemma ATPase of Arabidopsis thaliana. The 66-kD polypeptide cross-reacted with monoclonal antibodies raised to the 70-kD subunit of the vacuolar H+-ATPase of oat roots. The functional molecular size of the tonoplast H+-ATPase, analyzed in situ by radiation inactivation, was found to be around 400 kD. The 66-kD subunit of the tonoplast H+…

0106 biological sciencesPhysiologyATPaseProtein subunitPlant ScienceVacuole01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health scienceschemistry.chemical_compoundHydroxylamineProton transport[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGenetics030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyAcer pseudoplatanusbiology.organism_classificationEnzymechemistryBiochemistryPolyclonal antibodiesbiology.protein010606 plant biology & botanyResearch Article
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An isoleucine residue within the carboxyl-transferase domain of multidomain acetyl-coenzyme A carboxylase is a major determinant of sensitivity to ar…

2003

Abstract A 3,300-bp DNA fragment encoding the carboxyl-transferase domain of the multidomain, chloroplastic acetyl-coenzyme A carboxylase (ACCase) was sequenced in aryloxyphenoxypropionate (APP)-resistant and -sensitive Alopecurus myosuroides (Huds.). No resistant plant contained an Ile-1,781-Leu substitution, previously shown to confer resistance to APPs and cyclohexanediones (CHDs). Instead, an Ile-2,041-Asn substitution was found in resistant plants. Phylogenetic analysis of the sequences revealed that Asn-2,041 ACCase alleles derived from several distinct origins. Allele-specific polymerase chain reaction associated the presence of Asn-2,041 with seedling resistance to APPs but not to C…

0106 biological sciencesPhysiologyMolecular Sequence DataSequence alignmentPlant ScienceBiology01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants geneticschemistry.chemical_compoundMagnoliopsida[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsmental disordersGeneticsTransferaseVULPINAmino Acid SequenceIsoleucinePeptide sequencePhylogenyComputingMilieux_MISCELLANEOUS2. Zero hungerchemistry.chemical_classificationPolymorphism GeneticCyclohexanonesHerbicidesAcetyl-CoA carboxylase04 agricultural and veterinary sciencesACETYL-COA CARBOXYLASEPyruvate carboxylaseProtein Structure TertiaryEnzymeBiochemistrychemistryMutation040103 agronomy & agriculture0401 agriculture forestry and fisheriesIsoleucinePropionatesSequence AlignmentDNA010606 plant biology & botanyResearch Article
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Distinct lytic vacuolar compartments are embedded inside the protein storage vacuole of dry and germinating Arabidopsis thaliana seeds.

2011

International audience; Plant cell vacuoles are diverse and dynamic structures. In particular, during seed germination, the protein storage vacuoles are rapidly replaced by a central lytic vacuole enabling rapid elongation of embryo cells. In this study, we investigate the dynamic remodeling of vacuolar compartments during Arabidopsis seed germination using immunocytochemistry with antibodies against tonoplast intrinsic protein (TIP) isoforms as well as proteins involved in nutrient mobilization and vacuolar acidification. Our results confirm the existence of a lytic compartment embedded in the protein storage vacuole of dry seeds, decorated by γ-TIP, the vacuolar proton pumping pyrophospha…

0106 biological sciencesPhysiologyProtein storage vacuoleProton-pumping pyrophosphataseArabidopsisPlant ScienceVacuoleUNIQUEMESH: Protein Isoforms01 natural sciencesPYROPHOSPHATASEArabidopsisProtein IsoformsMESH: ArabidopsisH+-ATPASETONOPLAST INTRINSIC PROTEINPLANT-CELLSCation Transport ProteinsIN-VIVOPlant Proteinschemistry.chemical_classification0303 health sciencesMESH: Plant ProteinsGeneral MedicineCell biologyProtein TransportVacuolar acidificationLytic cycleSeedsPREVACUOLAR COMPARTMENTMESH: DesiccationVacuolar Proton-Translocating ATPasesMESH: Protein TransportMESH: Vacuolar Proton-Translocating ATPasesGerminationMESH: Arabidopsis ProteinsMESH: GerminationBiologyAquaporinsMESH: Vacuoles03 medical and health sciencesMESH: AquaporinsMESH: Cation Transport ProteinsStorage protein[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyLytic vacuoleDesiccation030304 developmental biologySeedArabidopsis ProteinsCell Biologybiology.organism_classificationTRANSPORTchemistryMESH: SeedsVacuolesVacuoleMEMBRANEMOBILIZATION010606 plant biology & botany
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Reticulon-like proteins in Arabidopsis thaliana: structural organization and ER localization

2007

International audience; Reticulons are proteins that have been found predominantly associated with the endoplasmic reticulum in yeast and mammalian cells. While their functions are still poorly understood, recent findings suggest that they participate in the shaping of the tubular endoplamic reticulum (ER). Although reticulon-like proteins have been identified in plants, very little is known about their cellular localization and functions. Here, we characterized the reticulon-like protein family of Arabidopsis thaliana. Three subfamilies can be distinguished on the basis of structural organization and sequence homology. We investigated the subcellular localization of two members of the larg…

0106 biological sciencesProtein familyMolecular Sequence DataBiophysicsArabidopsis[SDV.BC]Life Sciences [q-bio]/Cellular BiologyRTLNB01 natural sciencesBiochemistryPlant Epidermis03 medical and health sciencesProtein structureStructural BiologyArabidopsisGeneticsArabidopsis thalianaAmino Acid SequenceMolecular BiologyCellular localizationConserved SequencePhylogeny030304 developmental biology0303 health sciencesbiologySequence Homology Amino AcidArabidopsis ProteinsEndoplasmic reticulumENDOPLASMIC RETICULUMCHLOROPLASTARABIDOPSIS THALIANACell BiologySubcellular localizationbiology.organism_classificationRETICULONBiochemistryReticulonRETICULON-LIKE PROTEIN BSequence Alignment010606 plant biology & botany
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