Search results for "binding proteins"

showing 10 items of 911 documents

Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

2005

A new potential light-harvesting protein, named Lhca5, was recently detected in higher plants. Because of the low amount of Lhca5 in thylakoid membranes, the isolation of a native Lhca5 pigment-protein complex has not been achieved to date. Therefore, we used in vitro reconstitution to analyze whether Lhca5 binds pigments and is actually an additional light-harvesting protein. By this approach we could demonstrate that Lhca5 binds pigments in a unique stoichiometry. Analyses of pigment requirements for light-harvesting complex formation by Lhca5 revealed that chlorophyll b is the only indispensable pigment. Fluorescence measurements showed that ligated chlorophylls and carotenoids are arran…

ChlorophyllChlorophyll bPigment bindingArabidopsisLight-Harvesting Protein Complexesmacromolecular substancesBiologyPhotosystem IBiochemistryFluorescencechemistry.chemical_compoundProtein structureProtein Structure QuaternaryMolecular BiologyPhotosystemPhotosystem I Protein ComplexArabidopsis ProteinsPigments BiologicalCell BiologyCarotenoidsFluorescenceBiochemistrychemistryThylakoidChlorophyll Binding ProteinsChlorophyll Binding ProteinsDimerizationJournal of Biological Chemistry
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Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-…

2007

Photosynthetic light-harvesting complexes (LHCs) are assembled from apoproteins (Lhc proteins) and non-covalently attached pigments. Despite a considerable amino acid sequence identity, these proteins differ in their oligomerization behavior. To identify the amino acid residues determining the heterodimerization of Lhca1 and Lhca4 to form LHCI-730, we mutated the poorly conserved second transmembrane helix of the two subunits. Mutated genes were expressed in Escherichia coli and the resultant proteins were refolded in vitro and subsequently analyzed by gel electrophoresis. Replacement of the entire second helix in Lhca4 by the one of Lhca3 abolished heterodimerization, whereas it had no eff…

ChlorophyllModels MolecularMolecular Sequence DataLight-Harvesting Protein ComplexesBiologyProtein Structure SecondarySerineSolanum lycopersicumStructural BiologyChlorophyll bindingConsensus sequenceHistidineHomology modelingAmino Acid SequenceAmino AcidsProtein Structure QuaternaryMolecular BiologyPeptide sequenceHistidinePlant Proteinschemistry.chemical_classificationPhotosystem I Protein ComplexAmino acidTransmembrane domainProtein SubunitschemistryBiochemistryMutagenesisChlorophyll Binding ProteinsDimerizationSequence AlignmentJournal of molecular biology
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TFIIH Operates through an Expanded Proximal Promoter To Fine-Tune c-myc Expression

2004

A continuous stream of activating and repressing signals is processed by the transcription complex paused at the promoter of the c-myc proto-oncogene. The general transcription factor IIH (TFIIH) is held at promoters prior to promoter escape and so is well situated to channel the input of activators and repressors to modulate c-myc expression. We have compared cells expressing only a mutated p89 (xeroderma pigmentosum complementation group B [XPB]), the largest TFIIH subunit, with the same cells functionally complemented with the wild-type protein (XPB/wt-p89). Here, we show structural, compositional, and functional differences in transcription complexes between XPB and XPB/wt-89 cells at t…

Chromatin ImmunoprecipitationDNA ComplementaryCell SurvivalUltraviolet RaysBlotting WesternGreen Fluorescent ProteinsGene ExpressionRepressorCellular homeostasisBiologyTransfectionModels BiologicalProto-Oncogene MasProto-Oncogene Proteins c-mycTranscription Factors TFIIRibonucleasesPotassium PermanganateTranscription (biology)HumansRNA MessengerPromoter Regions GeneticMolecular BiologyModels GeneticGeneral transcription factorCell CycleGenetic Complementation TestDNA HelicasesPromoterCell BiologyFibroblastsFlow CytometryMolecular biologyDNA-Binding ProteinsKineticsTranscription Factor TFIIHMicroscopy FluorescenceMutationTranscription preinitiation complexTranscription factor II HTranscription Factor TFIIHPlasmidsMolecular and Cellular Biology
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Satb2 Regulates Callosal Projection Neuron Identity in the Developing Cerebral Cortex

2008

SummarySatb2 is a DNA-binding protein that regulates chromatin organization and gene expression. In the developing brain, Satb2 is expressed in cortical neurons that extend axons across the corpus callosum. To assess the role of Satb2 in neurons, we analyzed mice in which the Satb2 locus was disrupted by insertion of a LacZ gene. In mutant mice, β-galactosidase-labeled axons are absent from the corpus callosum and instead descend along the corticospinal tract. Satb2 mutant neurons acquire expression of Ctip2, a transcription factor that is necessary and sufficient for the extension of subcortical projections by cortical neurons. Conversely, ectopic expression of Satb2 in neural stem cells m…

Chromatin ImmunoprecipitationNeuroscience(all)Electrophoretic Mobility Shift AssayMice TransgenicNerve Tissue ProteinsDEVBIOBiologyCorpus callosumMOLNEUROMiceNeural PathwaysmedicineAnimalsCells CulturedCerebral CortexNeuronsRegulation of gene expressionStem CellsGeneral NeuroscienceGene Expression Regulation DevelopmentalMatrix Attachment Region Binding ProteinsDNAEmbryo MammalianNeural stem cellChromatinmedicine.anatomical_structureAnimals NewbornBromodeoxyuridinenervous systemCerebral cortexRegulatory sequenceMutationCorticospinal tractEctopic expressionNeuroscienceTranscription Factors
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RIP-Chip analysis supports different roles for AGO2 and GW182 proteins in recruiting and processing microRNA targets.

2019

Background MicroRNAs (miRNAs) are small non-coding RNA molecules mediating the translational repression and degradation of target mRNAs in the cell. Mature miRNAs are used as a template by the RNA-induced silencing complex (RISC) to recognize the complementary mRNAs to be regulated. To discern further RISC functions, we analyzed the activities of two RISC proteins, AGO2 and GW182, in the MCF-7 human breast cancer cell line. Methods We performed three RIP-Chip experiments using either anti-AGO2 or anti-GW182 antibodies and compiled a data set made up of the miRNA and mRNA expression profiles of three samples for each experiment. Specifically, we analyzed the input sample, the immunoprecipita…

Chromatin ImmunoprecipitationSupport Vector MachineRIP-Chip data analysisMiRNA bindingComputational biologyBiologylcsh:Computer applications to medicine. Medical informaticsBiochemistryAutoantigens03 medical and health sciencesOpen Reading Frames0302 clinical medicineStructural BiologymicroRNARIP-Chip data analysiCoding regionGene silencingHumansRNA MessengerMolecular BiologyGenelcsh:QH301-705.5030304 developmental biology0303 health sciencesBinding SitesApplied MathematicsGene Expression ProfilingResearchRNARNA-Binding ProteinsmicroRNA target predictionRISC proteins AGO2 and GW182Computer Science ApplicationsSettore BIO/18 - GeneticaMicroRNAslcsh:Biology (General)Gene Expression Regulation030220 oncology & carcinogenesismicroRNA regulatory activityArgonaute ProteinsMCF-7 Cellslcsh:R858-859.7DNA microarrayRIP-ChipBMC bioinformatics
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ORGANIZATION OF HIGHER-LEVEL CHROMATIN STRUCTURES (CHROMOMERE, CHROMONEMA AND CHROMATIN BLOCK) EXAMINED USING VISIBLE LIGHT-INDUCED CHROMATIN PHOTO-S…

2002

The method of chromatin photo-stabilization by the action of visible light in the presence of ethidium bromide was used for investigation of higher-level chromatin structures in isolated nuclei. As a model we used rat hepatocyte nuclei isolated in buffers which stabilized or destabilized nuclear matrix. Several higher-level chromatin structures were visualized: 100 nm globules—chromomeres, chains of chromomeres—chromonemata, aggregates of chromomeres—blocks of condensed chromatin. All these structures were completely destroyed by 2 M NaCl extraction independent of the matrix state, and DNA was extruded from the residual nuclei (nuclear matrices) into a halo. These results show that nuclear …

ChromomereLightPhotochemistrySolenoid (DNA)BuffersBiologyRadiation Dosagechemistry.chemical_compoundMicroscopy Electron TransmissionNuclear Matrix-Associated ProteinsEthidiumAnimalsNucleoidChromatin structure remodeling (RSC) complexInterphaseCell NucleusCell BiologyGeneral MedicineNuclear matrixMolecular biologyChromatinProtein Structure TertiaryRatsChromatinDNA-Binding ProteinschemistryHepatocytesBiophysicsbiology.proteinInterphaseDNASubcellular FractionsCell Biology International
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MicroRNA-Based Therapeutic Perspectives in Myotonic Dystrophy

2019

Myotonic dystrophy involves two types of chronically debilitating rare neuromuscular diseases: type 1 (DM1) and type 2 (DM2). Both share similarities in molecular cause, clinical signs, and symptoms with DM2 patients usually displaying milder phenotypes. It is well documented that key clinical symptoms in DM are associated with a strong mis-regulation of RNA metabolism observed in patient’s cells. This mis-regulation is triggered by two leading DM-linked events: the sequestration of Muscleblind-like proteins (MBNL) and the mis-regulation of the CUGBP RNA-Binding Protein Elav-Like Family Member 1 (CELF1) that cause significant alterations to their important functions in RNA processing. It ha…

Context (language use)miRNA-based drugReviewBioinformaticsMyotonic dystrophyCatalysislcsh:ChemistryInorganic ChemistryMBNL proteinsCELF1microRNADrug DiscoveryMedicineAnimalsHumansPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyCELF1 ProteinRna processingmyotonic dystrophymicroRNAbusiness.industryOrganic ChemistryAlternative splicingmiRNA-targeting drugRNA-Binding ProteinsGeneral MedicineGenetic Therapymedicine.diseasePhenotypeComputer Science ApplicationsAlternative SplicingMicroRNAslcsh:Biology (General)lcsh:QD1-999Drug developmentGene Expression Regulationantisense oligonucleotidesbusinessFunction (biology)International Journal of Molecular Sciences
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The structural plasticity of the C terminus of p21Cip1 is a determinant for target protein recognition.

2003

The cyclin-dependent kinase inhibitory protein p21(Cip1) might play multiple roles in cell-cycle regulation through interaction of its C-terminal domain with a defined set of cellular proteins such as proliferating cell nuclear antigen (PCNA), calmodulin (CaM), and the oncoprotein SET. p21(Cip1) could be described as an intrinsically unstructured protein in solution although the C-terminal domain adopts a well-defined extended conformation when bound to PCNA. However, the molecular mechanism of the interaction with CaM and the oncoprotein SET is not well understood, partly because of the lack of structural information. In this work, a peptide derived from the C-terminal domain of p21(Cip1) …

Cyclin-Dependent Kinase Inhibitor p21Models MolecularMagnetic Resonance SpectroscopyCalmodulinChromosomal Proteins Non-HistoneProtein ConformationPeptideBiologyLigandsBiochemistryBinding CompetitiveDomain (software engineering)Molecular recognitionCalmodulinCyclinsProliferating Cell Nuclear AntigenEscherichia coliHumansHistone ChaperonesMolecular Biologychemistry.chemical_classificationC-terminusCircular DichroismOrganic ChemistryCell CycleProteinsPeptide FragmentsCell biologyDNA-Binding ProteinschemistryBiochemistrybiology.proteinMolecular MedicineTarget proteinAlpha helixBinding domainTranscription FactorsChembiochem : a European journal of chemical biology
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Benzo[a]pyrene represses DNA repair through altered E2F1/E2F4 function marking an early event in DNA damage-induced cellular senescence

2020

AbstractTranscriptional regulation of DNA repair is of outmost importance for the restoration of DNA integrity upon genotoxic stress. Here we report that the potent environmental carcinogen benzo[a]pyrene (B[a]P) activates a cellular DNA damage response resulting in transcriptional repression of mismatch repair (MMR) genes (MSH2, MSH6, EXO1) and of RAD51, the central homologous recombination repair (HR) component, ultimately leading to downregulation of MMR and HR. B[a]P-induced gene repression is caused by abrogated E2F1 signalling. This occurs through proteasomal degradation of E2F1 in G2-arrested cells and downregulation of E2F1 mRNA expression in G1-arrested cells. Repression of E2F1-me…

Cyclin-Dependent Kinase Inhibitor p21SenescenceAcademicSubjects/SCI00010DNA repairDNA damageRAD51E2F4 Transcription FactorBiologyDNA Mismatch Repair03 medical and health sciences0302 clinical medicineCell Line TumorBenzo(a)pyreneGeneticsHumansCellular SenescenceCell Line Transformed030304 developmental biology0303 health sciencesGene regulation Chromatin and EpigeneticsRecombinational DNA RepairEpithelial CellsKv Channel-Interacting ProteinsCell Cycle CheckpointsDNAFibroblastsCell biologyDNA-Binding ProteinsRepressor ProteinsMSH6DNA Repair EnzymesExodeoxyribonucleasesMutS Homolog 2 ProteinGamma RaysMSH2030220 oncology & carcinogenesisCarcinogensMCF-7 CellsDNA mismatch repairRad51 RecombinaseCell agingE2F1 Transcription FactorDNA DamageSignal TransductionNucleic Acids Research
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Presentation of an Immunodominant Immediate-Early CD8+ T Cell Epitope Resists Human Cytomegalovirus Immunoevasion.

2013

Control of human cytomegalovirus (HCMV) depends on CD8+ T cell responses that are shaped by an individual's repertoire of MHC molecules. MHC class I presentation is modulated by a set of HCMV-encoded proteins. Here we show that HCMV immunoevasins differentially impair T cell recognition of epitopes from the same viral antigen, immediate-early 1 (IE-1), that are presented by different MHC class I allotypes. In the presence of immunoevasins, HLA-A- and HLA-B-restricted T cell clones were ineffective, but HLA-C*0702-restricted T cell clones recognized and killed infected cells. Resistance of HLA-C*0702 to viral immunoevasins US2 and US11 was mediated by the alpha3 domain and C-terminal region …

Cytomegalovirus InfectionMaleViral DiseasesvirusesCytomegalovirusEpitopes T-LymphocyteNK cellsAdaptive ImmunityCD8-Positive T-LymphocytesMajor Histocompatibility ComplexInterleukin 21Viral Envelope ProteinsCytotoxic T celllcsh:QH301-705.5Antigen PresentationbiologyViral Immune EvasionImmune cellsRNA-Binding ProteinsInnate ImmunityKiller Cells Naturalmedicine.anatomical_structureInfectious DiseasesCytomegalovirus InfectionsMedicineFemaleResearch Articlelcsh:Immunologic diseases. AllergyT cellImmunologyCD1T cells610StreptamerMicrobiologyImmediate-Early ProteinsImmunomodulationViral ProteinsVirologyMHC class IGeneticsmedicineHumansAntigen-presenting cellMolecular BiologyBiologyImmune EvasionHistocompatibility Antigens Class IImmunityMHC restrictionVirologyProtein Structure Tertiarylcsh:Biology (General)Immunologybiology.proteinParasitologylcsh:RC581-607
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