Search results for "histones"

showing 10 items of 200 documents

RNA-binding ability of PIPP in requires the entire protein

2003

Post-transcriptional fate of eukaryotic mRNAs depends on association with different classes of RNA-binding proteins (RBPs). Among these proteins, the cold-shock domain (CSD)-containing proteins, also called Y-box proteins, play a key role in controlling the recruitment of mRNA to the translational machinery, in response to environmental cues, both in development and in differentiated cells. We recently cloned a rat cDNA encoding a new CSD-protein that we called PIPPin. This protein also contains two putative double-stranded RNA-binding motifs (PIP(1) and PIP(2)) flanking the central CSD, and is able to bind mRNAs encoding H1 degrees and H3.3 histone variants. In order to clarify the role of…

Protein FoldingNerve Tissue ProteinsSequence alignmentRNA-binding proteinPlasma protein bindingArticleRNA-binding proteinscold-shock domainPIPPinhistone variantsHistonesSettore BIO/10 - BiochimicaComplementary DNAHistone H2AAnimalsRNA MessengerGeneticsMessenger RNAbiologyRNA-Binding ProteinsRNACell BiologyRecombinant ProteinsProtein Structure TertiaryRatsCell biologyHistoneGene Expression Regulationbiology.proteinMolecular MedicineSequence AlignmentProtein BindingJournal of Cellular and Molecular Medicine
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Telomerase and Telomere Length in Pulmonary Fibrosis

2013

In addition to its expression in stem cells and many cancers, telomerase activity is transiently induced in murine bleomycin (BLM)-induced pulmonary fibrosis with increased levels of telomerase transcriptase (TERT) expression, which is essential for fibrosis. To extend these observations to human chronic fibrotic lung disease, we investigated the expression of telomerase activity in lung fibroblasts from patients with interstitial lung diseases (ILDs), including idiopathic pulmonary fibrosis (IPF). The results showed that telomerase activity was induced in more than 66% of IPF lung fibroblast samples, in comparison with less than 29% from control samples, some of which were obtained from lu…

Pulmonary and Respiratory MedicineMaleTelomerasePathologymedicine.medical_specialtyClinical BiochemistryBiologyBleomycinGene Expression Regulation EnzymologicHistonesTelomerase RNA componentIdiopathic pulmonary fibrosischemistry.chemical_compoundBleomycinMiceFibrosisPulmonary fibrosismedicineAnimalsHumansEmfisema pulmonarPromoter Regions GeneticMolecular BiologyLungTelomeraseCells CulturedMice KnockoutLungAntibiotics AntineoplasticAcetylationCell BiologyArticlesFibroblastsTelomererespiratory systemmedicine.diseaseIdiopathic Pulmonary FibrosisTelomereUp-Regulationrespiratory tract diseasesmedicine.anatomical_structurechemistryPulmonsChronic DiseaseCancer researchFemaleAlveolitis Extrinsic AllergicPulmons Malalties
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Cyclic AMP-induced Chromatin Changes Support the NFATc-mediated Recruitment of GATA-3 to the Interleukin 5 Promoter

2008

Elevated intracellular cyclic AMP levels, which suppress the proliferation of naive T cells and type 1 T helper (Th1) cells are a property of T helper 2 (Th2) cells and regulatory T cells. While cyclic AMP signals interfere with the IL-2 promoter induction, they support the induction of Th2-type genes, in particular of il-5 gene. We show here that cyclic AMP signals support the generation of three inducible DNase I hypersensitive chromatin sites over the il-5 locus, including its promoter region. In addition, cyclic AMP signals enhance histone H3 acetylation at the IL-5 promoter and the concerted binding of GATA-3 and NFATc to the promoter. This is facilitated by direct protein-protein inte…

Quantitative Trait LociGATA3 Transcription FactorBiologyBiochemistryCell LineHistonesMiceTh2 CellsCyclic AMPTranscriptional regulationAnimalsHumansTranscription Chromatin and EpigeneticsPromoter Regions GeneticHistone H3 acetylationMolecular BiologyInterleukin 5Cell ProliferationMice Inbred BALB CNFATC Transcription FactorsEffectorLymphokineAcetylationZinc FingersPromoterCell BiologyDNA-binding domainTh1 CellsChromatin Assembly and DisassemblyMolecular biologyChromatinProtein Structure TertiaryChromatinGene Expression RegulationInterleukin-2Interleukin-5Signal TransductionJournal of Biological Chemistry
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Developing rat brain as well as cultured astrocytes contain H1° mRNA-protein complexes

2015

RNA-binding proteins (RBPs) regulate intracellular transport, pre-localization, stability, and translation of mRNAs [1]. We previously identified a set of proteins which interact with mRNAs encoding H1° and H3.3 histones [2-5]. All these proteins are probably part of a ribonucleoprotein particle [6]. Here we report the results of a more detailed study on the expression and intracellular localization of some of these RBPs, such as hnRNP K and A1, and Hsc70, during rat brain development and in cultured rat astrocytes. We also investigated the presence in the complexes of PIPPin/CSD-C2 protein. Affinity chromatography was performed as already described [6]. Preparation of total lysates and cel…

RNA-binding proteins (RBPs) H1° and H3.3 histones PIPPin/CSD-C2 protein cultured astrocytesSettore BIO/10 - BiochimicaSettore BIO/06 - Anatomia Comparata E Citologia
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DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair

2016

Abstract Repair of damaged DNA relies on the recruitment of DNA repair factors in a well orchestrated manner. As a prerequisite, the chromatin needs to be decondensed by chromatin remodelers to allow for binding of repair factors and for DNA repair to occur. Recent studies have implicated members of the SWI/SNF and INO80 families as well as PARP1 in nucleotide excision repair (NER). In this study, we report that the endonuclease DICER is implicated in chromatin decondensation during NER. In response to UV irradiation, DICER is recruited to chromatin in a ZRF1-mediated manner. The H2A–ubiquitin binding protein ZRF1 and DICER together impact on the chromatin conformation via PARP1. Moreover, …

Ribonuclease III0301 basic medicineDNA RepairUltraviolet RaysDNA damageDNA repairgenetic processesPoly (ADP-Ribose) Polymerase-1Genome Integrity Repair and ReplicationBiologyChromatin remodelingCell LineDEAD-box RNA HelicasesHistones03 medical and health scienceschemistry.chemical_compoundUbiquitinCell Line TumorGeneticsAnimalsHumansCaenorhabditis elegansOncogene ProteinsOsteoblastsUbiquitinfungiRNA-Binding ProteinsFibroblastsChromatin Assembly and DisassemblyMolecular biologyChromatinChromatinDNA-Binding Proteinsenzymes and coenzymes (carbohydrates)HEK293 Cells030104 developmental biologychemistrybiology.proteinDNADNA DamageMolecular ChaperonesNucleotide excision repairDicerNucleic Acids Research
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Quantification of Radiation Biomarkers in Leukocytes of Breast Cancer Patients Treated with Different Modalities of 3D-CRT or IMRT

2016

The goal of this study was to determine whether the quantification of radiation biomarkers in peripheral leukocytes of 111 breast cancer patients after adjuvant treatment with different modalities of three-dimensional conformal radiation therapy (3D-CRT) or intensity-modulated radiation therapy (IMRT) revealed any difference in the patients' radiation burden by out-of-field doses and an associated risk of second malignancies. Whole-breast radiation therapy was performed by 3D-CRT using either a hard wedge (n = 32) or a virtual wedge (n = 49) at dose rates of 3 and 6 Gy per min each. Patients receiving additional radiotherapy to lymph nodes were treated by 3D-CRT (n = 21) or IMRT (n = 9). DN…

Riskmedicine.medical_treatmentBiophysicsBreast Neoplasms030218 nuclear medicine & medical imagingHistones03 medical and health sciencesBasal (phylogenetics)0302 clinical medicineRadiation sensitivityBreast cancerLeukocytesmedicineHumansRadiology Nuclear Medicine and imagingChromosome AberrationsRadiationbusiness.industryDose-Response Relationship Radiationmedicine.diseasePeripheralRadiation therapy030220 oncology & carcinogenesisFemaleRadiotherapy Intensity-ModulatedLymphbusinessNuclear medicineAdjuvantBiomarkersEx vivoRadiation Research
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Yeast contains multiple forms of histone acetyltransferase.

1989

We have assayed several methods to quantitatively recover yeast histone acetyltransferases in an attempt to study the multiplicity of enzymatic activities. Two methods, namely (NH4)2SO4 precipitation and salt dissociation of chromatin in 0.5 M NaCl, yielded convenient preparations of total histone acetyltransferases. DEAE-Sepharose chromatography of the crude extracts resulted in the separation of three peaks of activity when total yeast histones were used as substrate. However, the scanning of the enzymatic activity toward individual histones along the chromatography, achieved by determining the specific activity of the individual histones after incubating whole histones and [14C]acetyl-Co…

Saccharomyces cerevisiae ProteinsIon chromatographySaccharomyces cerevisiaeBiochemistryHistone DeacetylasesSubstrate SpecificityHistonesAcetyltransferasesEnzyme StabilityHistone octamerMolecular BiologyHistone AcetyltransferasesHistone AcetyltransferasesChromatographybiologyChemistryAcetylationCell BiologyHistone acetyltransferaseChromatography Ion ExchangeYeastChromatinChromatinIsoenzymesKineticsHistoneBiochemistryAcetylationbiology.proteinThe Journal of biological chemistry
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Site specificity of pea histone acetyltransferase B in vitro.

1993

Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. The absence of modification of other potentially acetylatable sites i…

Saccharomyces cerevisiae ProteinsLysineMolecular Sequence DataBiochemistryChromatography AffinitySubstrate SpecificityHistone H4HistonesAffinity chromatographyAcetyltransferasesHistone octamerAmino Acid SequenceMolecular BiologyHistone AcetyltransferasesPlants MedicinalbiologyAcetylationFabaceaeCell BiologyHistone acetyltransferaseMolecular biologyIsoenzymesHistoneBiochemistryAcetylationHistone methyltransferasebiology.proteinElectrophoresis Polyacrylamide GelThe Journal of biological chemistry
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HAT1 and HAT2 Proteins Are Components of a Yeast Nuclear Histone Acetyltransferase Enzyme Specific for Free Histone H4

1998

We have analyzed the histone acetyltransferase enzymes obtained from a series of yeast hat1, hat2, and gcn5 single mutants and hat1,hat2 and hat1,gcn5 double mutants. Extracts prepared from both hat1 and hat2 mutant strains specifically lack the following two histone acetyltransferase activities: the well known cytoplasmic type B enzyme and a free histone H4-specific histone acetyltransferase located in the nucleus. The catalytic subunits of both cytoplasmic and nuclear enzymes have identical molecular masses (42 kDa), the same as that of HAT1. However, the cytoplasmic complex has a molecular mass (150 kDa) greater than that of the nuclear complex (110 kDa). The possible functions of HAT1 a…

Saccharomyces cerevisiae ProteinsMolecular Sequence DataSaccharomyces cerevisiaeBiologyBiochemistryCatalysisSubstrate SpecificityHistonesHistone H4Histone H1AcetyltransferasesHistone H2AHistone octamerMolecular BiologyHistone AcetyltransferasesCell NucleusHistone AcetyltransferasesBase SequenceAcetylationCell BiologyHistone acetyltransferaseMolecular WeightPhenotypeOligodeoxyribonucleotidesBiochemistryMutagenesisHistone methyltransferasebiology.proteinHAT1Journal of Biological Chemistry
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Protein Interactions within the Set1 Complex and Their Roles in the Regulation of Histone 3 Lysine 4 Methylation

2006

Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc…

Saccharomyces cerevisiae ProteinsProtein subunitLysineRNA polymerase IISaccharomyces cerevisiaeMethylationenvironment and public healthBiochemistryProtein–protein interactionHistonesSerineGene Expression Regulation FungalCoding regionMolecular BiologybiologyLysineHistone-Lysine N-MethyltransferaseCell BiologyMethylationDNA-Binding ProteinsProtein SubunitsHistoneBiochemistrybiology.proteinProtein BindingTranscription FactorsJournal of Biological Chemistry
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