Search results for " Post-Translational"

showing 10 items of 148 documents

Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellid Monorhaphis chuni.

2008

SUMMARYSilicateins, members of the cathepsin L family, are enzymes that have been shown to be involved in the biosynthesis/condensation of biosilica in spicules from Demospongiae (phylum Porifera), e.g. Tethya aurantium and Suberites domuncula. The class Hexactinellida also forms spicules from this inorganic material. This class of sponges includes species that form the largest biogenic silica structures on earth. The giant basal spicules from the hexactinellids Monorhaphis chuni and Monorhaphis intermedia can reach lengths of up to 3 m and diameters of 10 mm. The giant spicules as well as the tauactines consist of a biosilica shell that surrounds the axial canal, which harbours the axial f…

SpiculePhysiologyOceans and SeasMolecular Sequence DataAquatic ScienceCysteine Proteinase InhibitorsCathepsin LDemospongeSponge spiculeAnimalsAmino Acid SequenceTethya aurantiumMolecular BiologyEcology Evolution Behavior and SystematicsPhylogenyBinding SitesbiologyHexactinellidAnimal StructuresAnatomybiology.organism_classificationCathepsinsCystatinsPoriferaSuberites domunculaMolecular WeightSpongeBiochemistryInsect ScienceMolecular Probesbiology.proteinAnimal Science and ZoologyProtein Processing Post-TranslationalThe Journal of experimental biology
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Epigenetic Regulation of Early- and Late-Response Genes in Acute Pancreatitis

2015

Abstract Chromatin remodeling seems to regulate the patterns of proinflammatory genes. Our aim was to provide new insights into the epigenetic mechanisms that control transcriptional activation of early- and late-response genes in initiation and development of severe acute pancreatitis as a model of acute inflammation. Chromatin changes were studied by chromatin immunoprecipitation analysis, nucleosome positioning, and determination of histone modifications in promoters of proinflammatory genes in vivo in the course of taurocholate-induced necrotizing pancreatitis in rats and in vitro in rat pancreatic AR42J acinar cells stimulated with taurocholate or TNF-α. Here we show that the upregulat…

Taurocholic AcidTranscriptional Activation0301 basic medicineChromatin ImmunoprecipitationImmunologyAcinar CellsBiologyMethylationChromatin remodelingEpigenesis GeneticHistones03 medical and health sciences0302 clinical medicineHistone methylationAnimalsImmunology and AllergyNucleosomeEpigeneticsPromoter Regions GeneticEarly Growth Response Protein 1Histone AcetyltransferasesInflammationPancreatitis Acute NecrotizingTumor Necrosis Factor-alphaDNA HelicasesNuclear ProteinsAcetylationHistone acetyltransferaseChromatin Assembly and DisassemblyRatsChromatin030104 developmental biologyHistoneGene Expression Regulation030220 oncology & carcinogenesisbiology.proteinCancer researchProtein Processing Post-TranslationalChromatin immunoprecipitationTranscription FactorsThe Journal of Immunology
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Nucleosome-specific, Time-dependent Changes in Histone Modifications during Activation of the Early Growth Response 1 (Egr1) Gene

2014

Histone post-translational modifications and nucleosome remodeling are coordinate events involved in eukaryotic transcriptional regulation. There are relatively few data on the time course with which these events occur in individual nucleosomes. As a contribution to fill this gap, we first describe the nature and time course of structural changes in the nucleosomes -2, -1, and +1 of the murine Egr1 gene upon induction. To initiate the transient activation of the gene, we used the stimulation of MLP29 cells with phorbol esters and the in vivo activation after partial hepatectomy. In both models, nucleosomes -1 and +1 are partially evicted, whereas nucleosomes +1 and -2 slide downstream durin…

Time FactorsTranscription GeneticBiologyBiochemistryChromatin remodelingCell LineHistonesMiceHistone H1Histone methylationAnimalsHepatectomyHistone codeNucleosomeGene RegulationPromoter Regions GeneticMolecular BiologyEarly Growth Response Protein 1Mice KnockoutCell BiologyMolecular biologySWI/SNFLiver RegenerationNucleosomesCell biologyHistoneLiverChromatosomeHepatocytesbiology.proteinTetradecanoylphorbol AcetateProtein Processing Post-TranslationalJournal of Biological Chemistry
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Increased AICD generation does not result in increased nuclear translocation or activation of target gene transcription.

2008

A sequence of amyloid precursor protein (APP) cleavages culminates in the sequential release of the APP intracellular domain (AICD) and the amyloid beta peptide (Abeta) and/or p3 fragment. One of the environmental factors favouring the accumulation of AICD appears to be a rise in intracellular pH. Here we further identified the metabolism and subcellular localization of artificially expressed constructs under such conditions. We also co-examined the mechanistic lead up to the AICD accumulation and explored possible significances for its increased expression. We found that most of the AICD generated under pH neutralized conditions is likely cleaved from C83. While the AICD surplus was unable…

Transcriptional ActivationTranscription GeneticAmyloid betaActive Transport Cell NucleusCHO CellsModels BiologicalTransactivationAmyloid beta-Protein PrecursorCricetulusTranscription (biology)CricetinaeAmyloid precursor proteinAnimalsHumansLuciferaseCells CulturedRegulation of gene expressionCell NucleusbiologyCell BiologyHydrogen-Ion ConcentrationSubcellular localizationMolecular biologyCell biologyProtein Structure TertiaryCytosolbiology.proteinProtein Processing Post-TranslationalProtein BindingExperimental cell research
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Protease-mediated processing of Argonaute proteins controls small RNA association

2020

SummarySmall RNA pathways defend the germlines of animals against selfish genetic elements and help to maintain genomic integrity. At the same time, their activity needs to be well-controlled to prevent silencing of ‘self’ genes. Here, we reveal a proteolytic mechanism that controls endogenous small interfering (22G) RNA activity in the Caenorhabditis elegans germline to protect genome integrity and maintain fertility. We find that WAGO-1 and WAGO-3 Argonaute (Ago) proteins are matured through proteolytic processing of their unusually proline-rich N-termini. In the absence of DPF-3, a P-granule-localized N-terminal dipeptidase orthologous to mammalian DPP8/9, processing fails, causing a cha…

Transposable elementSmall RNAanimal structuresDNA damageBiologyDipeptidyl peptidaseSubstrate Specificity03 medical and health sciences0302 clinical medicineAnimalsGene silencingRNA MessengerRNA Small InterferingCaenorhabditis elegansCaenorhabditis elegans ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMolecular BiologyGeneCaenorhabditis elegans030304 developmental biology0303 health sciencesWild typeRNACell BiologyArgonautebiology.organism_classificationCell biologyFertilityArgonaute ProteinsProteolysisRNA HelminthProtein Processing Post-Translational030217 neurology & neurosurgery
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Tributyltin(Iv) butyrate: A novel epigenetic modifier with er stress-and apoptosis-inducing properties in colon cancer cells

2021

Organotin(IV) compounds are a class of non-platinum metallo-conjugates exhibiting antitumor activity. The effects of different organotin types has been related to several mechanisms, including their ability to modify acetylation protein status and to promote apoptosis. Here, we focus on triorganotin(IV) complexes of butyric acid, a well-known HDAC inhibitor with antitumor properties. The conjugated compounds were synthesized and characterised by FTIR spectroscopy, multi-nuclear (1H, 13C and 119Sn) NMR, and mass spectrometry (ESI-MS). In the triorganotin(IV) complexes, an anionic monodentate butyrate ligand was observed, which coordinated the tin atom on a tetra-coordinated, monomeric enviro…

Triorganotin(IV) butyratesPharmaceutical ScienceOrganic chemistryApoptosisButyrateArticleHistone DeacetylasesAnalytical ChemistryEpigenesis GeneticButyric acidchemistry.chemical_compoundQD241-441HDAC inhibitorsCell Line TumorSettore BIO/10 - BiochimicaDrug DiscoveryHumansPhysical and Theoretical ChemistrybiologyAcetylationLigand (biochemistry)Endoplasmic Reticulum StressColon cancerHistonechemistryBiochemistryHistone acetylationChemistry (miscellaneous)ApoptosisAcetylationSettore CHIM/03 - Chimica Generale E InorganicaColonic NeoplasmsTributyltinbiology.proteinUnfolded protein responseMolecular MedicineButyric AcidTrialkyltin CompoundsER stressProtein Processing Post-Translational
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NMR structure of a non-conjugatable, ADP-ribosylation associated, ubiquitin-like domain from Tetrahymena thermophila polyubiquitin locus.

2019

Abstract Background Ubiquitin-like domains (UbLs), in addition to being post-translationally conjugated to the target through the E1-E2-E3 enzymatic cascade, can be translated as a part of the protein they ought to regulate. As integral UbLs coexist with the rest of the protein, their structural properties can differ from canonical ubiquitin, depending on the protein context and how they interact with it. In this work, we investigate T.th-ubl5, a UbL present in a polyubiquitin locus of Tetrahymena thermophila, which is integral to an ADP-ribosyl transferase protein. Only one other co-occurrence of these two domains within the same protein has been reported. Methods NMR, multiple sequence al…

UBL DOMAINspektroskopiaGTPasePARKINBiochemistryPROTEIN BACKBONEACTIVATIONprotein-protein interaction0302 clinical medicineProtein-protein interactionUbiquitinmolekyylidynamiikkaNMR-spektroskopiaPolyubiquitinADP Ribose Transferases0303 health sciencesMultiple sequence alignmentbiologyFERM domainChemistryTetrahymenastructure-function relationshipFAMILYCell biologyRECEPTORSPost-translational modificationSignal TransductionBiophysicsSequence alignmentMolecular Dynamics SimulationUbiquitin-like domainsMECHANISMSProtein–protein interactionTetrahymena thermophila03 medical and health sciencesNMR spectroscopyADP-RibosylationubikitiinitMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologyMolecular dynamics simulationsStructure-function relationshipmolecular dynamics simulationsbiology.organism_classificationProtein Structure Tertiarypost-translational modificationProteasomeMOLECULAR-DYNAMICSbiology.protein1182 Biochemistry cell and molecular biologyproteiinitGTPASEProtein Processing Post-Translational030217 neurology & neurosurgeryFERM DOMAINBiochimica et biophysica acta. General subjects
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Regulation of NOS expression in vascular diseases

2020

Nitric oxide synthases (NOS) are the major sources of nitric oxide (NO), a small bioactive molecule involved in the regulation of many cellular processes. One of the most prominent functions of NO is regulation of vasodilatation and thereby control of blood pressure. Most important for vascular tone is NOS3. Endothelial NOS3-generated NO diffuses into the vascular smooth muscle cells, activates the soluble guanylate cyclase resulting in enhanced cGMP concentrations and smooth muscle cell relaxation. However, more and more evidence exist that also NOS1 and NOS2 contribute to vascular function. We summarize the current knowledge about the regulation of NOS expression in the vasculature by tra…

Vascular smooth muscleNitric Oxide Synthase Type IIINOS1CellNitric Oxide Synthase Type IIBlood PressureVasodilationInflammationNitric Oxide Synthase Type INitric OxideMuscle Smooth VascularNitric oxidechemistry.chemical_compoundmedicineAnimalsHumansProtein IsoformsVascular DiseasesRNA Processing Post-TranscriptionalInflammationRegulation of gene expressionInnate immune systemAtherosclerosisImmunity InnateCell biologyGene Expression Regulation Neoplasticmedicine.anatomical_structurechemistryNitric Oxide Synthasemedicine.symptomProtein Processing Post-TranslationalFrontiers in Bioscience-Landmark
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Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
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Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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