Search results for "Proteolysi"

showing 10 items of 119 documents

Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale Methods

2020

We present a detailed theoretical analysis of the reaction mechanism of proteolysis catalyzed by the main protease of SARS-CoV-2. Using multiscale simulation methods, we have characterized the interactions established by a peptidic substrate in the active site, and then we have explored the free energy landscape associated with the acylation and deacylation steps of the proteolysis reaction, characterizing the transition states of the process. Our mechanistic proposals can explain most of the experimental observations made on the highly similar ortholog protease of SARS-CoV. We point to some key interactions that may facilitate the acylation process and thus can be crucial in the design of …

Proteolysismedicine.medical_treatmentComputational biology010402 general chemistry01 natural sciencesQM/MMCatalysisAcylationQM/MM3CL proteaseMolecular dynamicsminimum free energy pathmedicineacylationProteasebiologymedicine.diagnostic_test010405 organic chemistryChemistrySARS-CoV-2deacylationfungiActive siteEnergy landscapeGeneral ChemistryTransition statemolecular dynamics0104 chemical sciencesbiology.proteinResearch ArticleACS Catalysis
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The Abundant Tegument Protein pUL25 of Human Cytomegalovirus Prevents Proteasomal Degradation of pUL26 and Supports Its Suppression of ISGylation

2018

The tegument of human cytomegalovirus (HCMV) virions contains proteins that interfere with both the intrinsic and the innate immunity. One protein with a thus far unknown function is pUL25. The deletion of pUL25 in a viral mutant (Towne-ΔUL25) had no impact on the release of virions and subviral dense bodies or on virion morphogenesis. Proteomic analyses showed few alterations in the overall protein composition of extracellular particles. A surprising result, however, was the almost complete absence of pUL26 in virions and dense bodies of Towne-ΔUL25 and a reduction of the large isoform pUL26-p27 in mutant virus-infected cells. pUL26 had been shown to inhibit protein conjugation with the in…

Proteomics0301 basic medicineIntrinsic immunityHuman cytomegalovirusImmunoprecipitationvirusesImmunologyMutantCytomegalovirusBiologyVirus ReplicationMicrobiologyViral Matrix ProteinsViral Proteins03 medical and health sciencesInterferonVirologymedicineHumansUbiquitinsCells CulturedInnate immune systemvirus diseasesViral tegumentFibroblastsbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseISG15Immunity InnateVirus-Cell InteractionsCell biology030104 developmental biologyInsect ScienceMutationProteolysisCytokinesmedicine.drugJournal of Virology
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Purification and partial characterization of a lectin protein complex, the clathrilectin, from the calcareous sponge Clathrina clathrus

2016

Carbohydrate-binding proteins were purified from the marine calcareous sponge Clathrina clathrus via affinity chromatography on lactose and N-acetyl glucosamine- agarose resins. Proteomic analysis of acrylamide gel separated protein subunits obtained in reducing conditions pointed out several candidates for lectins. Based on amino- acid sequence similarity, two peptides displayed homology with the jack bean lectin Concanavalin A, 
 including a conserved domain shared by proteins in the L-type lectin superfamily. An N-acetyl glucosamine - binding protein complex, named clathrilectin, was further purified via gel filtration chromatography, bioguided with a diagnostic rabbit erythrocyte haemag…

Proteomics0301 basic medicinePhysiologySyconBiochemistry03 medical and health sciencesAffinity chromatographyLectinsAnimalsTrypsinMolecular Biology030102 biochemistry & molecular biologybiologyCalcareous spongeHemagglutinationLectinClathrina clathrusbiology.organism_classificationMolecular biologyCell aggregationPoriferaPorifera ; Clathrina clathrus ; lectin ; N-acetyl-glucosamine ; cell aggregation ; proteomicsSponge030104 developmental biologyBiochemistryConcanavalin AProteolysisbiology.proteinCarbohydrate MetabolismFemaleRabbitsComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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Stuck at work? Quantitative proteomics of environmental wine yeast strains reveals the natural mechanism of overcoming stuck fermentation

2015

During fermentation oenological yeast cells are subjected to a number of different stress conditions and must respond rapidly to the continuously changing environment of this harsh ecological niche. In this study we gained more insights into the cell adaptation mechanisms by linking proteome monitoring with knowledge on physiological behaviour of different strains during fermentation under model winemaking conditions. We used 2D-DIGE technology to monitor the proteome evolution of two newly discovered environmental yeast strains Saccharomyces bayanus and triple hybrid Saccharomyces cerevisiae × Saccharomyces kudriavzevii × S. bayanus and compared them to data obtained for the commercially a…

Proteomics0301 basic medicineProteomeSaccharomyces cerevisiaeSaccharomyces bayanusWineSaccharomyces cerevisiaeBiologyBiochemistrySaccharomycesFungal ProteinsTwo-Dimensional Difference Gel ElectrophoresisSaccharomyces03 medical and health sciencesStress PhysiologicalAmino AcidsMolecular BiologyEthanolCell redox homeostasisbiology.organism_classificationYeastStuck fermentationBiosynthetic PathwaysProtein TransportYeast in winemaking030104 developmental biologyBiochemistryFermentationProteolysisGlycolysisOxidation-ReductionSaccharomyces kudriavzeviiPROTEOMICS
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Identification of Rothia Bacteria as Gluten-Degrading Natural Colonizers of the Upper Gastro-Intestinal Tract

2011

Background Gluten proteins, prominent constituents of barley, wheat and rye, cause celiac disease in genetically predisposed subjects. Gluten is notoriously difficult to digest by mammalian proteolytic enzymes and the protease-resistant domains contain multiple immunogenic epitopes. The aim of this study was to identify novel sources of gluten-digesting microbial enzymes from the upper gastro-intestinal tract with the potential to neutralize gluten epitopes. Methodology/Principal Findings Oral microorganisms with gluten-degrading capacity were obtained by a selective plating strategy using gluten agar. Microbial speciations were carried out by 16S rDNA gene sequencing. Enzyme activities wer…

ProteomicsApplied Microbiologylcsh:MedicineBiochemistryGliadinEpitopeSubstrate SpecificityUpper Gastrointestinal Tractlcsh:ScienceBifidobacterium2. Zero hungerchemistry.chemical_classification0303 health sciencesAniline CompoundsMultidisciplinarymedicine.diagnostic_testbiologyHydrolysisProteolytic enzymesfood and beveragesHydrogen-Ion ConcentrationEnzymes3. Good healthSolutionsBiochemistryMedical MicrobiologyMedicineSmall IntestineResearch ArticleProteasesGlutensProteolysisMolecular Sequence DataDental PlaqueGastroenterology and HepatologyMicrobiologydigestive systemMicrobiology03 medical and health sciencesAntigenmedicineHumansAmino Acid SequenceSalivaBiology030304 developmental biologyBinding Sites030306 microbiologylcsh:Rnutritional and metabolic diseasesbiology.organism_classificationGlutenPeptide Fragmentsdigestive system diseasesMolecular WeightCeliac DiseasechemistryProteolysisbiology.proteinlcsh:QGliadinMicrococcaceaePLoS ONE
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The Wnt-specific astacin proteinase HAS-7 restricts head organizer formation in Hydra

2021

Abstract Background The Hydra head organizer acts as a signaling center that initiates and maintains the primary body axis in steady state polyps and during budding or regeneration. Wnt/beta-Catenin signaling functions as a primary cue controlling this process, but how Wnt ligand activity is locally restricted at the protein level is poorly understood. Here we report a proteomic analysis of Hydra head tissue leading to the identification of an astacin family proteinase as a Wnt processing factor. Results Hydra astacin-7 (HAS-7) is expressed from gland cells as an apical-distal gradient in the body column, peaking close beneath the tentacle zone. HAS-7 siRNA knockdown abrogates HyWnt3 proteo…

ProteomicsPhysiologyHydraQH301-705.5XenopusPlant ScienceProteinaseGeneral Biochemistry Genetics and Molecular BiologyStructural BiologyAstacinAxis formationAnimalsRNA Small InterferingBiology (General)Wnt Signaling PathwayEcology Evolution Behavior and SystematicsActinbeta CateninBody PatterningGene knockdownBuddingbiologyRegeneration (biology)Wnt signaling pathwayMetalloendopeptidasesCell Biologybiology.organism_classificationWnt signalingCell biologyWnt ProteinsProteolysisLernaean HydraAstacinGeneral Agricultural and Biological SciencesHeadDevelopmental BiologyBiotechnologyResearch ArticleBMC Biology
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Production of biologically active light chain of tetanus toxin inEscherichia coli

1993

AbstractThe activity of the light (L) chain of tetanus toxin, and of mutants constructed by site-directed mutagenesis, was studied by expression and purification of the proteins from E. coli. Wild-type recombinant L chain (pTet87) was active in the inhibition of exocytosis from cultured bovine adrenal chromaffin cells, although at a level 5–15% of that of L chain purified from tetanus toxin. L chain mutants which terminated at Leu-438 (pTet89), or which contained a Cys-to-Ser mutation at residue 439 (pTet88) were equally as active as the full-length recombinant protein. The reduced activity of pTet87 L chain correlated with C-terminal proteolysis of the protein upon purification. A tryptic …

Recombinant proteinMacromolecular SubstancesProteolysisMolecular Sequence DataRestriction MappingDNA RecombinantBiophysicsBiologymedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosislaw.inventionNorepinephrineTetanus ToxinStructural BiologylawEscherichia coliGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularSite-directed mutagenesisMolecular BiologyEscherichia coliCells Culturedchemistry.chemical_classificationBase Sequencemedicine.diagnostic_testToxinBiological activityCell BiologyMolecular biologyRecombinant ProteinsE. coli Chromaffin cellAmino acidKineticsOligodeoxyribonucleotideschemistryBiochemistryAdrenal MedullaMutagenesis Site-DirectedRecombinant DNACalciumCattleElectrophoresis Polyacrylamide GelSite directed mutagenesisFEBS Letters
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Compromised nuclear envelope integrity drives TREX1-dependent DNA damage and tumor cell invasion

2021

Although mutations leading to a compromised nuclear envelope cause diseases such as muscular dystrophies or accelerated aging, the consequences of mechanically induced nuclear envelope ruptures are less known. Here, we show that nuclear envelope ruptures induce DNA damage that promotes senescence in non-transformed cells and induces an invasive phenotype in human breast cancer cells. We find that the endoplasmic reticulum (ER)-associated exonuclease TREX1 translocates into the nucleus after nuclear envelope rupture and is required to induce DNA damage. Inside the mammary duct, cellular crowding leads to nuclear envelope ruptures that generate TREX1-dependent DNA damage, thereby driving the …

SenescenceExonucleaseDNA damageNuclear Envelope[SDV]Life Sciences [q-bio]Breast NeoplasmsBiologySettore MED/08 - Anatomia PatologicaGeneral Biochemistry Genetics and Molecular BiologyCell LineMicemedicineSettore MED/05 - Patologia ClinicaAnimalsHumansNeoplasm InvasivenessEpithelial–mesenchymal transitionCellular SenescenceEndoplasmic reticulumPhosphoproteinsXenograft Model Antitumor AssaysCell biology[SDV] Life Sciences [q-bio]medicine.anatomical_structureExodeoxyribonucleasesCancer cellProteolysisbiology.proteinTREX1 nuclear envelope rupture DNA damage mammary duct carcinoma tumor invasion senescence breast cancer cGAS confinement epithelial to mesenchymal transition Animals Breast Neoplasms Cell Line Cellular Senescence Collagen Disease Progression Exodeoxyribonucleases Female Humans Mice Neoplasm InvasivenessNuclear Envelope PhosphoproteinsProteolysis Xenograft Model Antitumor Assays DNA DamageDisease ProgressionFemaleCollagenNucleusExtracellular Matrix DegradationDNA Damage
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Synthetic lethal metabolic targeting of cellular senescence in cancer therapy.

2013

Activated oncogenes and anticancer chemotherapy induce cellular senescence, a terminal growth arrest of viable cells characterized by S-phase entry-blocking histone 3 lysine 9 trimethylation (H3K9me3). Although therapy-induced senescence (TIS) improves long-term outcomes, potentially harmful properties of senescent tumour cells make their quantitative elimination a therapeutic priority. Here we use the Eµ-myc transgenic mouse lymphoma model in which TIS depends on the H3K9 histone methyltransferase Suv39h1 to show the mechanism and therapeutic exploitation of senescence-related metabolic reprogramming in vitro and in vivo. After senescence-inducing chemotherapy, TIS-competent lymphomas but …

SenescenceMaleLymphoma B-CellTransgeneApoptosisMice TransgenicMiceUbiquitinStress PhysiologicalAutophagyAnimalsCaspase 12Cellular SenescenceMultidisciplinarybiologyCaspase 3Endoplasmic reticulumAutophagyEndoplasmic Reticulum StressSurvival RateDisease Models AnimalHistoneGlucoseBiochemistryHistone methyltransferaseProteolysisUnfolded protein responsebiology.proteinCancer researchFemaleNature
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Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin

1993

Staphylococcal alpha-toxin is a single-chain polypeptide with a molecular weight of 34,000 that hexamerizes in lipid bilayers to form pores of 1-1.5 nm effective diameter in membranes. We demonstrate that limited proteolysis of purified alpha-toxin with proteinase K generates a hemolytically active product that yields one major protein band of 17-18 kDa in SDS-polyacrylamide gel electrophoresis. The 17-18-kDa protein band harbors two major fragments of similar size representing the N- and C-terminal halves, which remain associated with each other in non-denaturing buffers but dissociate in 6 M urea. Dissociation in urea leads to loss of hemolytic activity. In contrast, unnicked alpha-toxin …

Staphylococcus aureusLysisProteolysisBacterial ToxinsHemolysin ProteinsHemolysisBiochemistryMonocytesCell membraneHemolysin ProteinsmedicineHumansLymphocytesLipid bilayerMolecular BiologyGel electrophoresismedicine.diagnostic_testbiologyCell MembraneErythrocyte MembraneSerine EndopeptidasesCell BiologyProteinase KPeptide FragmentsKineticsMembranemedicine.anatomical_structureBiochemistryChromatography Gelbiology.proteinElectrophoresis Polyacrylamide GelEndopeptidase KJournal of Biological Chemistry
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