Search results for "Protein Complex"

showing 10 items of 154 documents

Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.

2014

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification…

ProteomicsSaccharomyces cerevisiae Proteinslcsh:QH426-470Saccharomyces cerevisiaeBiochemistryMolecular GeneticsRNA TransferGene Expression Regulation FungalMolecular Cell BiologyGeneticsFungal GeneticsPhosphorylationPost-Translational ModificationUridineMolecular BiologyAdaptor Proteins Signal TransducingHistone AcetyltransferasesAlanineSpectrometric Identification of ProteinsBiology and life sciencesCasein Kinase INucleotidesMicrobial GeneticsProteinsCell BiologyPeptide Elongation Factorslcsh:GeneticsPhenotypeMultiprotein ComplexesRNAMolecular ComplexesTransfer RNAAnticodonsResearch ArticlePLoS genetics
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Arabidopsis p24δ5 and p24δ9 facilitate Coat Protein I-dependent transport of the K/HDEL receptor ERD2 from the Golgi to the endoplasmic reticulum.

2014

The p24 proteins belong to a family of type I membrane proteins which cycle between the endoplasmic reticulum (ER) and Golgi via coat protein I (COPI) and COPII vesicles. Current nomenclature classifies them into four subfamilies, although plant p24 proteins belong to either the p24β or the p24δ subfamilies. Here, we show that Arabidopsis p24δ5/δ9 and HDEL ligands shift the steady-state distribution of the K/HDEL receptor ERD2 from the Golgi to the ER. We also show that p24δ5/δ9 interact directly with ERD2. This interaction requires the Golgi dynamics (GOLD) domain in p24δ5 and is much higher at acidic than at neutral pH, consistent with both proteins interacting at the cis-Golgi. In additi…

Receptors PeptideArabidopsisGolgi ApparatusPlant ScienceBiologyEndoplasmic ReticulumCoat Protein Complex Isymbols.namesakeGeneticsAnimalsSecretionCOPIIVesicular-tubular clusterArabidopsis ProteinsEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusCell biologyTransport proteinDNA-Binding ProteinsProtein TransportMembrane proteinsymbolsTranscription FactorsThe Plant journal : for cell and molecular biology
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Identification of a β-Dystroglycan Immunoreactive Subcompartment in Photoreceptor Terminals

2005

PURPOSE Mutations in the dystrophin-associated glycoprotein complex (DGC) cause various forms of muscular dystrophy. These diseases are characterized by progressive loss of skeletal muscle tissue and by dysfunctions in the central nervous system (CNS). The CNS deficits include an altered electroretinogram, caused by an impaired synaptic transmission between photoreceptors and their postsynaptic target cells in the outer plexiform layer (OPL). The DGC is concentrated in the OPL but its exact distribution is controversial. Therefore, the precise distribution of beta-dystroglycan, the central component of the DGC, within the OPL of the mature chick retina, was determined. METHODS Double immuno…

Retinal Bipolar Cellsgenetic structuresPresynaptic TerminalsOuter plexiform layerNerve Tissue ProteinsRetinal Horizontal CellsNeurotransmissionRibbon synapseImaging Three-DimensionalGlycoprotein complexImage Processing Computer-AssistedmedicineDystroglycanAnimalsActive zoneDystroglycansFluorescent Antibody Technique IndirectSynaptic ribbonRetinabiologyAnatomyCell CompartmentationCell biologyMicroscopy Electronmedicine.anatomical_structureMicroscopy Fluorescencebiology.proteinsense organsChickensPhotoreceptor Cells VertebrateInvestigative Opthalmology & Visual Science
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Promoter architecture and transcriptional regulation of Abf1-dependent ribosomal protein genes inSaccharomyces cerevisiae

2016

In Saccharomyces cerevisiae, ribosomal protein gene (RPG) promoters display binding sites for either Rap1 or Abf1 transcription factors. Unlike Rap1-associated promoters, the small cohort of Abf1-dependent RPGs (Abf1-RPGs) has not been extensively investigated. We show that RPL3, RPL4B, RPP1A, RPS22B and RPS28A/B share a common promoter architecture, with an Abf1 site upstream of a conserved element matching the sequence recognized by Fhl1, a transcription factor which together with Ifh1 orchestrates Rap1-associated RPG regulation. Abf1 and Fhl1 promoter association was confirmed by ChIP and/or gel retardation assays. Mutational analysis revealed a more severe requirement of Abf1 than Fhl1 …

Ribosomal Proteins0301 basic medicineSaccharomyces cerevisiae ProteinsTranscription GeneticTelomere-Binding ProteinsRibosome biogenesisSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Biology03 medical and health sciencesRibosomal proteinTranscription (biology)Gene Expression Regulation FungalGeneticsTranscriptional regulationBinding sitePromoter Regions GeneticTranscription factorGeneGeneticsBinding SitesTOR Serine-Threonine KinasesGene regulation Chromatin and EpigeneticsForkhead Transcription FactorsPromoterDNA-Binding Proteins030104 developmental biologyMultiprotein ComplexesTrans-ActivatorsTranscription FactorsNucleic Acids Research
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Regulation of the hDlg/hScrib/Hugl-1 tumour suppressor complex.

2008

The proper function of the Scribble tumour suppressor complex is dependent upon the correct localisation of its components. Previously we observed dynamic relocalisation of the hDlg component under conditions of osmotic stress. We now show that the other two components of the complex, hScrib and Hugl-1 display similar patterns of expression. We demonstrate, by shRNA ablation of hScrib expression, that hDlg and Hugl-1 are in part dependent upon hScrib for their correct localization. However under conditions of osmotic stress this apparent dependency no longer exists: hDlg and Hugl-1 localise to cell membranes independently of hScrib. We also demonstrate an interaction between the three compo…

SCRIBBlotting WesternBiologylaw.inventionCell LineSmall hairpin RNADiscs Large Homolog 1 ProteinlawSyntaxinAnimalsHumansSorbitolTransport VesiclesAdaptor Proteins Signal TransducingRegulation of gene expressionQa-SNARE ProteinsTumor Suppressor ProteinsOsmolar ConcentrationSignal transducing adaptor proteinMembrane ProteinsCell BiologyTransport proteinCell biologyVesicular transport proteinCytoskeletal ProteinsProtein TransportGene Expression RegulationMultiprotein ComplexesSuppressorRNA InterferenceSignal TransductionExperimental cell research
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Rtp1p Is a Karyopherin-Like Protein Required for RNA Polymerase II Biogenesis

2013

The assembly and nuclear transport of RNA polymerase II (RNA pol II) are processes that require the participation of many auxiliary factors. In a yeast genetic screen, we identified a previously uncharacterized gene, YMR185w (renamed RTP1), which encodes a protein required for the nuclear import of RNA pol II. Using protein affinity purification coupled to mass spectrometry, we identified interactions between Rtp1p and members of the R2TP complex. Rtp1p also interacts, to a different extent, with several RNA pol II subunits. The pattern of interactions is compatible with a role for Rtp1p as an assembly factor that participates in the formation of the Rpb2/Rpb3 subassembly complex and its bi…

Saccharomyces cerevisiae ProteinsActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeKaryopherinsBiologyGene Expression Regulation FungalTranscriptional regulationRNA polymerase IProtein Interaction MapsMolecular BiologyRNA polymerase II holoenzymeR2TP complexGeneticsNuclear cap-binding protein complexArticlesCell BiologyPhosphoproteinsUp-RegulationCell biologyNuclear Pore Complex Proteinsbiology.proteinRNA Polymerase IITranscription factor II DCarrier ProteinsGene DeletionSmall nuclear RNATranscription Factors
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Physical and Genetic Interactions Link the Yeast Protein Zds1p with mRNA Nuclear Export

2005

Eukaryotic gene expression requires the export of mRNA from the nucleus to the cytoplasm. The DEAD box protein Dbp5p is an essential export factor conserved from yeast to man. A fraction of Dbp5p forms a complex with nucleoporins of the cytoplasmic filaments of the nuclear pore complex. Gfd1p was identified originally as a multicopy suppressor of the rat8-2 ts allele of DBP5. Here we reported that Dbp5p and Gfd1p interact with Zds1p, a protein previously identified as a multicopy suppressor in several yeast genetic screens. By using the two-hybrid system, we showed that Zds1p interacts in vivo with both Gfd1p and Dbp5p. In vitro binding experiments revealed that Gfd1p and Dbp5p bind directl…

Saccharomyces cerevisiae ProteinsMolecular Sequence DataMutantActive Transport Cell NucleusSaccharomyces cerevisiaeBiologyBiochemistryCytosolGene expressionmedicineRNA MessengerNuclear poreNuclear export signalMolecular BiologyAdaptor Proteins Signal TransducingDNA PrimersGeneticsMessenger RNABase SequenceNuclear cap-binding protein complexRNA FungalCell BiologyCell biologyCell nucleusmedicine.anatomical_structureNucleoporinGenome FungalJournal of Biological Chemistry
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Melanoma cells release extracellular vesicles which contain RNA-binding proteins able to bind the mRNA encoding histone H1°

2015

Extracellular vesicles (EVs) are produced by most prokaryotic and eukaryotic cells; tumour cells, however, release much higher amounts of EVs, which contain cancer-specific proteins and RNAs. Molecules carried by EVs are captured by surrounding cells, which then undergo profound phenotypic modifications. G26/24 oligodendroglioma cells release, for example, EVs containing FasL and TRAIL, which induce apoptosis in rat cortical neurons and astrocytes in culture. By metabolic labelling of cells, EV-mediated horizontal transfer of radioactive proteins was clearly demonstrated. Among the proteins present in EVs produced by oligodendroglioma cells, extracellular matrix remodelling proteases, and t…

Settore BIO/10 - BiochimicaSettore BIO/06 - Anatomia Comparata E CitologiaExtracellular vesicles (EVs) G26/24 oligodendroglioma cells xtracellular matrix remodelling proteases A375 melanoma cells H1° histone RNA-protein complexes myelin expression factor-2 (MYEF2)
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Identification of N- and C-terminal Amino Acids of Lhca1 and Lhca4 Required for Formation of the Heterodimeric Peripheral Photosystem I Antenna LHCI-…

2002

Apoproteins of higher plant light-harvesting complexes (LHC) share considerable amino acid sequence identity/similarity. Despite this fact, they occur in different oligomeric states (i.e., monomeric, dimeric, and trimeric). As a step toward understanding the underlying structure requirements for different oligomerization behavior, we analyzed whether amino acids at the N- and C-termini of Lhca1 and Lhca4 are involved in the formation of the heterodimeric LHCI-730. Using altered proteins produced by deletion or site-directed mutagenesis for reconstitution, we were able to identify amino acids required for the assembly of LHCI-730. At the N-terminus of Lhca1, W4 is involved in heterodimerizat…

StereochemistryDimerPhotosynthetic Reaction Center Complex ProteinsMutantLight-Harvesting Protein ComplexesBiologyPhotosystem IBiochemistrychemistry.chemical_compoundResidue (chemistry)Point MutationAmino AcidsPeptide sequencePlant ProteinsSequence Deletionchemistry.chemical_classificationPhotosystem I Protein ComplexArabidopsis ProteinsMutagenesisRecombinant ProteinsAmino acidMonomerBiochemistrychemistryChlorophyll Binding ProteinsDimerizationBiochemistry
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Modular organization in the reductive evolution of protein-protein interaction networks

2006

Analysis of the reduction in genome size of Buchnera aphidicola from its common ancestor E. coli shows that the organization of networks into modules is the property that seems to be directly related with the evolutionary process of genome reduction.

Systems biologyComplex systemComputational biologyBiologyGenomeProtein protein interaction networkProtein–protein interactionBuchneraInteraction networkProtein Interaction MappingEscherichia coliAnimalsHumansDatabases ProteinGeneticsbusiness.industrySystems BiologyResearchbiochemical phenomena metabolism and nutritionModular designbiology.organism_classificationBiological EvolutionProtein Structure TertiaryStructural Homology ProteinMultiprotein ComplexesBuchnerabusinessAlgorithmsGenome BacterialGenome Biology
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