Search results for "Non-Histone"

showing 10 items of 33 documents

Immunohistochemical Study as a Tool in Differential Diagnosis of Pediatric Malignant Rhabdoid Tumor

2010

Malignant rhabdoid tumors (MRTs) are aggressive childhood neoplasms, occurring mainly in the kidney and brain. We describe 2 unusual cases of extrarenal and noncranial location (liver and soft tissue with dissemination) mimicking hepatoblastoma, neuroblastoma or Ewing sarcoma. Both cases revealed a polyphenotypic profile, combined with cytokeratin, vimentin, and CD99 expression. INI1/BAF-47 showed negative protein nuclear expression in both cases, suggesting a diagnosis of MRT. An extensive immunohistochemical panel was performed to exclude pediatric tumors reminiscent of MRT. The genetic studies failed to detected MYCN amplification, 11q23 deletion, and EWS break-apart positivity. No alter…

HepatoblastomaPathologymedicine.medical_specialtySkin NeoplasmsHistologyDesmoplastic small-round-cell tumorChromosomal Proteins Non-HistoneCD9912E7 AntigenN-Myc Proto-Oncogene ProteinPathology and Forensic MedicineDiagnosis DifferentialNeoplasms Multiple PrimaryFatal OutcomeAntigens CDNeuroblastomaAntineoplastic Combined Chemotherapy ProtocolsmedicineHumansVimentinRhabdoid TumorChromosome AberrationsOncogene ProteinsN-Myc Proto-Oncogene Proteinbusiness.industryLiver NeoplasmsInfant NewbornInfantNuclear ProteinsWilms' tumorSMARCB1 Proteinmedicine.diseaseImmunohistochemistryDNA-Binding ProteinsMedical Laboratory TechnologyDrug Resistance NeoplasmKeratinsFemaleSarcomaRNA-Binding Protein EWSDifferential diagnosisbusinessCell Adhesion MoleculesTranscription FactorsApplied Immunohistochemistry & Molecular Morphology
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A chromatin-associated protein from pea seeds preferentially binds histones H3 and H4

2002

Pisum sativum p16 is a protein present in the chromatin of ungerminated embryonic axes. The purification of p16 and the isolation of a cDNA clone of psp54, the gene encoding its precursor have been recently reported [Castillo, J., Rodrigo, M. I., Marquez, J. A., Zuniga, A and Franco, L. (2000) Eur. J. Biochem.267, 2156-2165]. In the present paper, we present data showing that p16 is a nuclear protein. First, after subcellular fractionation, p16 was clearly found in nuclei, although the protein is also present in other organelles. Immunocytochemical methods also confirm the above results. p16 seems to be firmly anchored to chromatin, as only extensive DNase I digestion of nuclei allows its r…

Histone-modifying enzymesNon-histone proteinHistoneBiochemistryHistone H1Histone methyltransferasebiology.proteinHistone codeBiologyChIP-on-chipBiochemistryChromatinEuropean Journal of Biochemistry
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Calcium-Dependent Assembly of Centrin-G-Protein Complex in Photoreceptor Cells

2002

Photoexcitation of rhodopsin activates a heterotrimeric G-protein cascade leading to cyclic GMP hydrolysis in vertebrate photoreceptors. Light-induced exchanges of the visual G-protein transducin between the outer and inner segment of rod photoreceptors occur through the narrow connecting cilium. Here we demonstrate that transducin colocalizes with the Ca(2+)-binding protein centrin 1 in a specific domain of this cilium. Coimmunoprecipitation, centrifugation, centrin overlay, size exclusion chromatography, and kinetic light-scattering experiments indicate that Ca(2+)-activated centrin 1 binds with high affinity and specificity to transducin. The assembly of centrin-G-protein complex is medi…

Lightgenetic structuresChromosomal Proteins Non-HistoneMacromolecular SubstancesImmunoprecipitationG proteinCentrifugationPlasma protein bindingBiologyRetinaSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinCalcium-binding proteinAnimalsScattering RadiationTransducinMicroscopy ImmunoelectronCell Growth and DevelopmentMolecular BiologyCalcium-Binding ProteinsCell BiologyHeterotrimeric GTP-Binding ProteinsPrecipitin TestsRatsCell biologyMice Inbred C57BLMolecular WeightRhodopsinCentrinChromatography Gelbiology.proteinCalciumCattlesense organsTransducinPhotoreceptor Cells VertebrateProtein BindingSignal TransductionMolecular and Cellular Biology
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Dppa3 expression is critical for generation of fully reprogrammed iPS cells and maintenance of Dlk1-Dio3 imprinting.

2014

Reprogramming of mouse somatic cells into induced pluripotent stem cells (iPSCs) often generates partially reprogrammed iPSCs (pre-iPSCs), low-grade chimera forming iPSCs (lg-iPSCs) and fully reprogrammed, high-grade chimera production competent iPSCs (hg-iPSCs). Lg-iPSC transcriptome analysis revealed misregulated Dlk1-Dio3 cluster gene expression and subsequently the imprinting defect at the Dlk1-Dio3 locus. Here, we show that germ-cell marker Dppa3 is present only in lg-iPSCs and hg-iPSCs, and that induction with exogenous Dppa3 enhances reprogramming kinetics, generating all hg-iPSCs, similar to vitamin C (Vc). Conversely, Dppa3-null fibroblasts show reprogramming block at pre-iPSCs sta…

MaleChromosomal Proteins Non-HistoneGreen Fluorescent ProteinsInduced Pluripotent Stem CellsMice TransgenicAscorbic AcidIodide PeroxidaseArticleGenomic ImprintingMiceAnimalsCrosses GeneticMice KnockoutGene Expression ProfilingCalcium-Binding ProteinsDNA MethylationFibroblastsMice Inbred C57BLRepressor ProteinsKineticsGerm CellsRetroviridaeGene Expression RegulationIntercellular Signaling Peptides and ProteinsFemaleProtein BindingNature communications
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Germline deletion of Cetn1 causes infertility in male mice

2013

Centrins are calmodulin-like Ca2+-binding proteins that can be found in all ciliated eukaryotic cells from yeast to mammals. Expressed in male germ cells and photoreceptors, centrin 1 (CETN1) resides in the photoreceptor transition zone and connecting cilium. To identify its function in mammals, we deleted Cetn1 by homologous recombination. Cetn1−/− mice were viable and showed no sign of retina degeneration suggesting that CETN1 is nonessential for photoreceptor ciliogenesis or structural maintenance. Phototransduction components localized normally to the Cetn1−/− photoreceptor outer segments, and loss of CETN1 had no effect on light-induced translocation of transducin to the inner segment.…

Maleendocrine systemLight Signal TransductionCentrioleChromosomal Proteins Non-HistoneSpermiogenesisBiologyMice03 medical and health sciencesRetinal Rod Photoreceptor CellsCiliogenesismedicineAnimalsBasal bodyTransducinSpermatogenesisGerm-Line MutationInfertility MaleCentriolesSequence Deletion030304 developmental biologyMice KnockoutGenetics0303 health sciencesSpermatidCalcium-Binding ProteinsCell Cycle030302 biochemistry & molecular biologyCell DifferentiationCell BiologySpermatidsCell biologyMice Inbred C57BLmedicine.anatomical_structureCentrinFemalesense organsTransducinResearch ArticleVisual phototransductionJournal of Cell Science
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Conserved chromosomal clustering of genes governed by chromatin regulators in Drosophila

2008

Transcriptional analysis of chromatin regulator mutants in Drosophila melanogaster identified clusters of functionally related genes conserved in other insect species.

Model organismsanimal structuresTranscription GeneticEvolutionChromosomal Proteins Non-HistoneDrosòfila melanogasterGenome studiesDevelopmentBiologyNon-histone proteinAnimalsDrosophila ProteinsDrosòfila -- GenèticaTranscription factorGeneGeneticsMicroarray analysis techniquesResearchGene Expression ProfilingMutació (Biologia)fungiNuclear Proteinsbiology.organism_classificationChromatin Assembly and DisassemblyChromatinHistoneDrosophila melanogasterDrosofila melanogasterGene Expression RegulationMultigene Familybiology.proteinDrosophila melanogasterDrosophila ProteinGenètica del desenvolupamentTranscription FactorsGenome Biology
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A multifunctional bicupin serves as precursor for a chromosomal protein of Pisum sativum seeds.

2005

The fact that the psp54 gene codes for p16, a seed chromatin protein of Pisum sativum, has been described previously. In the present paper it is shown that p54, the p16 precursor, also exists as a free polypeptide in pea and that it also yields p38, a second polypeptide from the N-terminal region of p54, which is co-localized at a subcellular level with p16. By using antibodies against pea p16 and p38, it was found that these proteins are present in the members of the tribe Viciae examined. Sequence analysis and 3D modelling indicates that p54 proteins belong to the cupin superfamily, and that they are related to sucrose binding proteins and, to a lesser extent, to vicilin-type seed storage…

Models MolecularPhysiologySequence analysisChromosomal Proteins Non-HistoneMolecular Sequence DataPlant ScienceResponse ElementsDNA-binding proteinPisumSativumGene Expression Regulation PlantSequence Analysis ProteinGene expressionStorage proteinAmino Acid SequenceRNA MessengerProtein PrecursorsPromoter Regions GeneticGenePlant Proteinschemistry.chemical_classificationMessenger RNAbiologyPeasfood and beveragesbiology.organism_classificationBiochemistrychemistryMultigene FamilyProtein BiosynthesisSeedsProtein Processing Post-TranslationalSequence AlignmentAbscisic AcidJournal of experimental botany
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Putative high mobility group non-histone chromosomal proteins from pea (Pisum sativum)

1991

Abstract Three putative HMG proteins, 1P, 2P and 3P have been isolated from pea ( Pisum sativum L. cv. Lincoln) nuclei by extraction with either 5% perchloric acid or 0.35 M NaCl and purified by preparative electrophoresis. The amino acid analysis showed many of the typical features of the HMG proteins, although 1P and 2P possess a somewhat reduced content of acidic amino acids and 3P has less than 20% basic amino acids. Peptide mapping with Staphylococcus aureus V8 protease suggested that none of the proteins are proteolytic products of histone H1.

Proteasebiologymedicine.medical_treatmentfood and beveragesPlant ScienceGeneral MedicineHmg proteinbiology.organism_classificationMolecular biologyPisumchemistry.chemical_compoundNon-histone proteinHigh-mobility groupSativumchemistryBiochemistryHistone H1GeneticsmedicinePMSFAgronomy and Crop SciencePlant Science
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The telomeric Cdc13-Stn1-Ten1 complex regulates RNA polymerase II transcription

2019

Advance article.

S phase transcribed genesTranscription GeneticChromosomal Proteins Non-HistoneCell Cycle ProteinsRNA polymerase IIBur1[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Genome Integrity Repair and ReplicationS Phase0302 clinical medicineTranscription (biology)Gene Expression Regulation FungalTranscriptional regulation0303 health sciencesCdc13-Stn1-Ten1biology030302 biochemistry & molecular biologyTranscription regulationRNA pol IIChromatinCyclin-Dependent KinasesCell biologyTelomeres030220 oncology & carcinogenesisRNA Polymerase IITranscriptional Elongation FactorsSaccharomyces cerevisiae ProteinsDNA polymerase IITelomere-Binding ProteinsSaccharomyces cerevisiae[SDV.CAN]Life Sciences [q-bio]/CancerSaccharomyces cerevisiaeCST complex03 medical and health sciencesGeneticsBudding yeastGenomesGene030304 developmental biologyHmo1RNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyPromoterbiology.organism_classificationCromosomesTelomerebiology.proteinSpt5Cyclin-Dependent Kinase-Activating Kinase
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Crystallization and preliminary X-ray studies of mouse centrin1.

2005

The expression, purification, crystallization and preliminary X-ray diffraction studies of mouse centrin1 are reported. Centrins belong to a family of Ca{sup 2+}-binding EF-hand proteins that play a fundamental role in centrosome duplication and the function of cilia. To shed light on the structure–function relationship of these proteins, mouse centrin1 has been crystallized. The mouse centrin1 has been expressed in Escherichia coli as a GST-centrin fusion protein containing a thrombin protease cleavage site between the fusion partners. Two constructs with different linking-sequence lengths were expressed and purified. Thrombin cleavage yielded functional centrin1 and N-terminally extended …

StereochemistryChromosomal Proteins Non-HistoneMolecular Sequence DataBiophysicsmacromolecular substancesCleavage (embryo)Crystallography X-RayBiochemistrylaw.inventionchemistry.chemical_compoundMiceStructure-Activity RelationshipThrombinStructural BiologylawGeneticsmedicineEscherichia coliAnimalsCentrosome duplicationAmino Acid SequenceCrystallizationDose-Response Relationship DrugCalcium-Binding ProteinsSpace groupCondensed Matter PhysicsFusion proteinRecombinant ProteinsCrystallographyenzymes and coenzymes (carbohydrates)KineticschemistryCrystallization CommunicationsX-ray crystallographybiological scienceshealth occupationsbacteriaCrystallizationEthylene glycolmedicine.drugActa crystallographica. Section F, Structural biology and crystallization communications
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