Search results for "Ligases"

showing 10 items of 72 documents

Three-dimensional structure of the anaphase-promoting complex.

2001

The anaphase-promoting complex (APC) is a cell cycle-regulated ubiquitin-protein ligase, composed of at least 11 subunits, that controls progression through mitosis and G1. Using cryo-electron microscopy and angular reconstitution, we have obtained a three-dimensional model of the human APC at a resolution of 24 A. The APC has a complex asymmetric structure 140 A x 140 A x 135 A in size, in which an outer protein wall surrounds a large inner cavity. We discuss the possibility that this cavity represents a reaction chamber in which ubiquitination reactions take place, analogous to the inner cavities formed by other protein machines such as the 26S proteasome and chaperone complexes. This cag…

Protein subunitUbiquitin-Protein LigasesAnaphase-Promoting Complex-CyclosomeLigasesProtein structureUbiquitinHumansProtein Structure QuaternaryMitosisMolecular Biologychemistry.chemical_classificationDNA ligasebiologyCryoelectron MicroscopyG1 PhaseUbiquitin-Protein Ligase ComplexesCell BiologyPrecipitin TestsCell biologyProtein Structure TertiaryProteasomechemistryChaperone (protein)biology.proteinAnaphase-promoting complexHeLa CellsMolecular cell
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Proteome-Wide Characterization of the RNA-Binding Protein RALY-Interactome Using the in Vivo-Biotinylation-Pulldown-Quant (iBioPQ) Approach

2013

RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No quantitative proteomic analysis of RALY-containing ribonucleoparticles (RNPs) has been performed so far, and the biological role of RALY remains elusive. Here, we present a workflow for the characterization of RALY's interaction partners, termed iBioPQ, that involves in vivo biotinylation of biotin acceptor peptide (BAP)-fused protein in the presence of the prokaryotic biotin holoenzyme synthetase of BirA so that it can be purified using streptavidin-coated magnetic beads, circumventing the need for specific antibodies and providing e…

ProteomeRecombinant Fusion ProteinsMolecular Sequence DataBiotinRNA-binding proteinBiologyHeterogeneous ribonucleoprotein particleProteomicsPoly(A)-Binding Protein IBiochemistryInteractomeELAV-Like Protein 103 medical and health scienceschemistry.chemical_compound0302 clinical medicineNuclear Matrix-Associated ProteinsBiotinProtein Interaction MappingHumansCarbon-Nitrogen LigasesAmino Acid SequenceProtein Interaction MapsPeptide sequence030304 developmental biology0303 health sciencesEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CRNA-Binding ProteinsGeneral ChemistryRepressor ProteinsHEK293 CellsELAV ProteinsGene Expression RegulationBiochemistrychemistryProtein Biosynthesis030220 oncology & carcinogenesisBiotinylationProteomeBiological AssayStreptavidinHeLa CellsProtein BindingJournal of Proteome Research
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Theileria parasites secrete a prolyl isomerase to maintain host leukocyte transformation

2015

Infectious agents develop intricate mechanisms to interact with host cell pathways and hijack their genetic and epigenetic machinery to change host cell phenotypic states. Among the Apicomplexa phylum of obligate intracellular parasites, which cause veterinary and human diseases, Theileria is the only genus that transforms its mammalian host cells. Theileria infection of bovine leukocytes induces proliferative and invasive phenotypes associated with activated signalling pathways, notably JNK and AP-1 (ref. 2). The transformed phenotypes are reversed by treatment with the theilericidal drug buparvaquone. We used comparative genomics to identify a homologue of the peptidyl-prolyl isomerase PI…

Proto-Oncogene Proteins c-jun[SDV]Life Sciences [q-bio]Drug ResistanceparasitesBiologyArticleCell LineHost-Parasite InteractionsmiR-155TheileriaTheileriaLeukocytesProlyl isomeraseAnimalsHumanscancerSecretionNIMA-Interacting Peptidylprolyl IsomeraseZebrafishComputingMilieux_MISCELLANEOUSPeptidylprolyl isomeraseSKP Cullin F-Box Protein LigasesMultidisciplinaryProtein StabilityGeneral CommentaryIntracellular parasiteUbiquitinationPeptidylprolyl Isomerasebiology.organism_classificationXenograft Model Antitumor AssaysMolecular biology3. Good healthCell biologyUbiquitin ligaseNIMA-Interacting Peptidylprolyl IsomeraseTranscription Factor AP-1Cell Transformation NeoplasticSchistosoma haematobiumPIN1biology.proteinMedicineCattleNaphthoquinonesSignal Transduction
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TOPORS, implicated in retinal degeneration, is a cilia-centrosomal protein.

2011

et al.

Retinal degenerationUbiquitin-Protein LigasesBiologymedicine.disease_causeRetinaCell Line03 medical and health scienceschemistry.chemical_compoundMiceNuclear proteins0302 clinical medicineIntraflagellar transportGeneticsmedicineBasal bodyAnimalsHumansPhotoreceptor CellsCiliaMolecular BiologyZebrafishGenetics (clinical)Cells CulturedZebrafish030304 developmental biologyCentrosome0303 health sciencesRetinaMutationUbiquitinCiliumRetinal DegenerationNuclear ProteinsRetinalTOPORS proteinGeneral MedicineArticlesmedicine.diseasebiology.organism_classification3. Good healthCell biologyNeoplasm ProteinsProtein Transportmedicine.anatomical_structurechemistryNeoplasm proteinssense organs030217 neurology & neurosurgeryHuman molecular genetics
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Partial purification and characterization of succinyl-CoA synthetase from Saccharomyces cerevisiae

1983

Succinyl-CoA synthetase from Saccharomyces cerevisiae was partially purified (20-fold) with a yield of 44%. The Michaelis-Menten constants were determined: Km (succinate) = 17 mM; Km (ATP) = 0.13 mM; Km (CoA) = 0.03 mM. The succinyl-CoA synthetase has a molecular weight of about 80000 dalton (as determined by polyacrylamide gradient gel electrophoresis). The pH optimum is at 6.0. During fermentation the activity of succinyl-CoA synthetase is lower than in aerobically grown yeast cells. The presence of succinyl-CoA synthetase in fermenting yeasts may be regarded as an indication for the oxidative formation of succinate. In fermenting yeast cells succinyl-CoA synthetase is repressed by glucos…

Saccharomyces cerevisiaeSuccinic AcidCatabolite repressionSaccharomyces cerevisiaeMicrobiologyAdenosine TriphosphateCoenzyme A LigasesSuccinate-CoA LigasesAnaerobiosisMolecular BiologyGel electrophoresischemistry.chemical_classificationChromatographybiologyorganic chemicalsSuccinyl coenzyme A synthetaseTemperatureSuccinatesSuccinate-CoA LigasesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationYeastAmino acidMolecular WeightKineticsBiochemistrychemistrybacteriaFermentationAntonie van Leeuwenhoek
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene

2021

This article belongs to the Section Cellular Biochemistry.

Salmonella typhimuriumTranscription GeneticNitrogen assimilationHaloferax mediterraneiGene ExpressionBiochemistryGlutamate-putrescine ligase activitySubstrate SpecificityLigasesAdenosine TriphosphateputrescineCloning MolecularPhylogenyhaloarchaeachemistry.chemical_classification0303 health sciencesbiologyChemistryHaloarchaeaEscherichia coli Proteinsglutamine synthetaseBioquímica y Biología MolecularQR1-502Recombinant ProteinsNitrogen assimilationHaloferax mediterraneiIsoenzymesBiochemistryArchaeal ProteinsGenetic VectorsGlutamic AcidGlutamate–putrescine ligaseMicrobiologyArticleglutamate–putrescine ligaseGlutamine synthetase03 medical and health sciencesAmmoniaGlutamine synthetaseNitrogen FixationEscherichia coliPutrescineAmino Acid SequenceMolecular Biology030304 developmental biologyDNA ligaseSequence Homology Amino Acid030306 microbiologyComputational Biologynitrogen assimilationbiology.organism_classificationMetabolic pathwayEnzymeProtein BiosynthesisHaloarchaeaGene Expression Regulation ArchaealSequence AlignmentBiomolecules
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Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina.

2005

Vinorine synthase (VS) is a central enzyme of the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure with significant sequence homology with VS is known. Crystals of VS and selenomethionyl-labelled VS from the medicinal plant Rauvolfia serpentina have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. VS crystals diffract to 2.8 Å and belong to space group P212121, with unit-cell parameters a = 82.3, b = 89.6, c = 136.2 Å. The selenomethionyl VS crystal was nearly isomorphous with the VS crystal.

StereochemistryCrystallography X-RayRauwolfialaw.inventionIndole AlkaloidsLigaseschemistry.chemical_compoundBiosynthesisStructural BiologylawRauvolfia serpentinamedicineCrystallizationSelenomethioninePlant ProteinsPEG 400chemistry.chemical_classificationATP synthasebiologyGeneral Medicinebiology.organism_classificationAjmalineEnzymechemistryAcyltransferasesbiology.proteinCrystallizationmedicine.drugActa crystallographica. Section D, Biological crystallography
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Protein Kinase C-dependent Ubiquitination and Clathrin-mediated Endocytosis of the Cationic Amino Acid Transporter CAT-1*

2011

Cationic amino acid transporter 1 (CAT-1) is responsible for the bulk of the uptake of cationic amino acids in most mammalian cells. Activation of protein kinase C (PKC) leads to down-regulation of the cell surface CAT-1. To examine the mechanisms of PKC-induced down-regulation of CAT-1, a functional mutant of CAT-1 (CAT-1-HA-GFP) was generated in which a hemagglutinin antigen (HA) epitope tag was introduced into the second extracellular loop and GFP was attached to the carboxyl terminus. CAT-1-HA-GFP was stably expressed in porcine aorthic endothelial and human epithelial kidney (HEK) 293 cells. Using the HA antibody internalization assay we have demonstrated that PKC-dependent endocytosis…

Swinemedia_common.quotation_subjectNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesUbiquitin-conjugating enzymeEndocytosisBiochemistryClathrinProtein Structure SecondaryMembrane BiologyAnimalsHumansAmino acid transporterInternalizationMolecular BiologyProtein kinase CProtein Kinase Cmedia_commonCationic Amino Acid Transporter 1biologyEndosomal Sorting Complexes Required for TransportUbiquitinationClathrin-Coated VesiclesCell BiologyReceptor-mediated endocytosisClathrinEndocytosisCell biologyUbiquitin ligaseHEK293 CellsBiochemistrybiology.protein
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The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity

2012

SummaryRIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or “translocon” containing RIG-I, 14-3-3ε, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3ε is essential for the stable inte…

TRIM25Cancer ResearchUbiquitin-Protein Ligasesviruseschemical and pharmacologic phenomenaHepacivirusMicrobiologyAntiviral AgentsModels BiologicalArticleCell LineDEAD-box RNA HelicasesTripartite Motif Proteins03 medical and health sciences0302 clinical medicineVirologyImmunology and Microbiology(all)Protein Interaction MappingHumansReceptors ImmunologicDEAD Box Protein 58Molecular Biology030304 developmental biology0303 health sciencesInnate immune systembiologyRIG-IRNAMembrane Proteinsvirus diseasesRNA virusbiochemical phenomena metabolism and nutritionbiology.organism_classificationTranslocon3. Good healthCell biology14-3-3 Proteins030220 oncology & carcinogenesisChaperone (protein)biology.proteinDEAD Box Protein 58Parasitologybiological phenomena cell phenomena and immunityMolecular ChaperonesProtein BindingTranscription FactorsCell Host & Microbe
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Oxidative stress, a new hallmark in the pathophysiology of Lafora progressive myoclonus epilepsy

2015

12 páginas, 4 figuras, 1 tabla

Ubiquitin-Protein LigasesFree radicalsBiologymedicine.disease_causeBiochemistryAntioxidantsLafora diseasechemistry.chemical_compoundLaforinPhysiology (medical)medicineHumansLafora diseaseProteostasis DeficienciesGlycogenAutophagyProtein Tyrosine Phosphatases Non-ReceptorMalinmedicine.diseaseOxidative StressProteostasisLafora DiseaseBiochemistrychemistryProteasomeOxidative stressMutationProteostasisUnfolded protein responseCarrier ProteinsLaforinGlycogenOxidative stressFree Radical Biology and Medicine
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