Search results for "Histone"

showing 10 items of 522 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
researchProduct

Identification in the rat brain of a set of nuclear proteins interacting with H1° mRNA

2012

Synthesis of H1° histone, in the developing rat brain, is also regulated at post-transcriptional level. Regulation of RNA metabolism depends on a series of RNA-binding proteins (RBPs); therefore, we searched for H1° mRNA-interacting proteins. With this aim, we used in vitro transcribed, biotinylated H1° RNA as bait to isolate, by a chromatographic approach, proteins which interact with this mRNA, in the nuclei of brain cells. Abundant RBPs, such as heterogeneous nuclear ribonucleoprotein (hnRNP) K and hnRNP A1, and molecular chaperones (heat shock cognate 70, Hsc70) were identified by mass spectrometry. Western blot analysis also revealed the presence of cold shock domain-containing protein…

Heterogeneous nuclear ribonucleoproteinRNA-binding proteinRNA-binding proteinBiologyenvironment and public healthHeterogeneous-Nuclear RibonucleoproteinsMass SpectrometryHistonesSettore BIO/10 - BiochimicaAnimalsRNA MessengerNuclear proteinRats WistarSettore BIO/06 - Anatomia Comparata E CitologiaRibonucleoproteinMessenger RNAPIPPinGeneral NeuroscienceRibonucleoprotein particleHSC70 Heat-Shock ProteinsRNABrainCSD-C2Molecular biologyCell biologyRatsHistonebiology.proteinH1° mRNAPost-transcriptional gene regulation
researchProduct

Type-II histone deacetylases: elusive plant nuclear signal transducers

2013

Since the beginning of the 21st century, numerous studies have concluded that the plant cell nucleus is one of the cellular compartments that define the specificity of the cellular response to an external stimulus or to a specific developmental stage. To that purpose, the nucleus contains all the enzymatic machinery required to carry out a wide variety of nuclear protein post-translational modifications (PTMs), which play an important role in signal transduction pathways leading to the modulation of specific sets of genes. PTMs include protein (de)acetylation which is controlled by the antagonistic activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Regarding p…

Histone AcetyltransferasesGeneticsPhysiologyPlant ScienceBiologyCell biologyHistoneAcetylationbiology.proteinNuclear proteinSignal transductionGeneCellular compartmentProtein deacetylationPlant, Cell & Environment
researchProduct

Redox signaling and histone acetylation in acute pancreatitis

2011

Histone acetylation via CBP/p300 coordinates the expression of proinflammatory cytokines in the activation phase of inflammation, particularly through mitogen-activated protein kinases (MAPKs), nuclear factor-κB (NF-κB), and signal transducers and activators of transcription (STAT) pathways. In contrast, histone deacetylases (HDACs) and protein phosphatases are mainly involved in the attenuation phase of inflammation. The role of reactive oxygen species (ROS) in the inflammatory cascade is much more important than expected. Mitochondrial ROS act as signal-transducing molecules that trigger proinflammatory cytokine production via inflammasome-independent and inflammasome-dependent pathways. …

Histone AcetyltransferasesMitochondrial ROSAcetylationProtein tyrosine phosphataseBiologyEndoplasmic Reticulum StressBiochemistryChromatin remodelingProinflammatory cytokineHistonesOxidative StressHistoneGene Expression RegulationPancreatitisAcetylationPhysiology (medical)Acute Diseasebiology.proteinCancer researchAnimalsHumansPhosphorylationOxidation-ReductionProtein Processing Post-TranslationalSignal TransductionFree Radical Biology and Medicine
researchProduct

Site specificity of yeast histone acetyltransferase B complex in vivo

2008

Saccharomyces cerevisiae Hat1, together with Hat2 and Hif1, forms the histone acetyltransferase B (HAT-B) complex. Previous studies performed with synthetic N-terminal histone H4 peptides found that whereas the HAT-B complex acetylates only Lys12, recombinant Hat1 is able to modify Lys12 and Lys5. Here we demonstrate that both Lys12 and Lys5 of soluble, non-chromatin-bound histone H4 are in vivo targets of acetylation for the yeast HAT-B enzyme. Moreover, coimmunoprecipitation assays revealed that Lys12/Lys5-acetylated histone H4 is bound to the HAT-B complex in the soluble cell fraction. Both Hat1 and Hat2, but not Hif1, are required for the Lys12/Lys5-specific acetylation and for histone …

Histone AcetyltransferasesbiologyCell BiologyHistone acetyltransferaseBiochemistryChromatinHistone H4Histone H3HistoneBiochemistryAcetylationparasitic diseasesbiology.proteinHAT1Molecular BiologyFEBS Journal
researchProduct

Histone H3 Lysine 4 Mono-methylation does not Require Ubiquitination of Histone H2B

2005

The yeast Set1-complex catalyzes histone H3 lysine 4 (H3K4) methylation. Using N-terminal Edman sequencing, we determined that 50% of H3K4 is methylated and consists of roughly equal amounts of mono, di and tri-methylated H3K4. We further show that loss of either Paf1 of the Paf1 elongation complex, or ubiquitination of histone H2B, has only a modest effect on bulk histone mono-methylation at H3K4. Despite the fact that Set1 recruitment decreases in paf1delta cells, loss of Paf1 results in an increase of H3K4 mono-methylation at the 5' coding region of active genes, suggesting a Paf1-independent targeting of Set1. In contrast to Paf1 inactivation, deleting RTF1 affects H3K4 mono-methylation…

Histone H3 Lysine 4UbiquitinLysineSaccharomyces cerevisiaeBiologyMethylationenvironment and public healthMolecular biologyCell biologyHistonesHistone H1Structural BiologyHistone methyltransferaseHistone H2AHistone methylationHistone H2BHistone codeHistone octamerMolecular BiologyJournal of Molecular Biology
researchProduct

Naturally occurring testis-specific histone H3 antisense transcripts inDrosophila

1997

While analysing the transcription of the cluster of cell-cycle regulated histone genes in Drosophila hydei, we have found transcripts spanned both histone H3 and H4 genes and were antisense for histone H3. As the two histone genes are in opposite orientation, these transcripts contained the sense strand of the histone H4 gene. Such transcripts were present in both poly(A) + and poly(A) - RNA fractions. The polyadenylated molecules contained a poly(A) tail at the 3' end of the stem-loop structure, which is characteristic for cell-cycle regulated histone mRNAs. The antisense RNA of histone H3 is synthesized exclusively in testes. By developing an improved protocol of in situ hybridization to …

Histone H4Histone H3Histone H1Histone methyltransferaseHistone methylationHistone H2AGeneticsCell BiologyBiologySAP30Molecular biologyDevelopmental BiologyAntisense RNAMolecular Reproduction and Development
researchProduct

A chromatin-associated histone deacetylase from pea (Pisum sativum)

1991

Abstract A histone deacetylase activity has been found in preparation of chromatin from pea (Pisum sativum) embryonic axes. This activity readily deacetylates free histones and is somewhat specific for H2A and H2B; this property and its chromatographic behaviour allowed us to identify the enzyme with the previously described histone deacetylase HD2 (Sendra et al., Plant Mol. Biol., 11 (1988) 857). HD2 is only loosely associated to chromatin but the enzymatic activity is enhanced when chromatin adopts a folded conformation. Polyamines and divalent cations activate the enzyme, probably due to their effect on chromatin folding.

Histone deacetylase 2HDAC10food and beveragesPlant ScienceGeneral MedicineBiologyChromatinHistone H1BiochemistryHistone methyltransferaseHistone H2AGeneticsHistone deacetylaseHistone deacetylase activityAgronomy and Crop SciencePlant Science
researchProduct

Distinct Site Specificity of Two Pea Histone Deacetylase Complexes

2001

We report on the site specificity of two intact pea histone deacetylase complexes. HD1 deacetylates lysines 5 and 16 of H4 in the order K16 > K5, while in the case of H3 the preferred order is K4 >> K18 approximately K9. The specificity of the HD2 complex is markedly different. The preferred residues in H4 are K8 approximately K5 > K16, while in H3 deacetylation, the complex HD2 prefers sites 4 and 18. To obtain these results, we have used a novel procedure based on the SPOT technique, a method to synthesize peptides on membrane supports. Different sets of membranes with sequentially overlapping histone peptides containing acetylated lysines in the sites corresponding to all in vivo acetyla…

Histone deacetylase 5Histone deacetylase 2ChemistryHDAC11HDAC10PeasSAP30BiochemistryHistone DeacetylasesSubstrate SpecificityBiochemistryHistone H2AHistone deacetylase complexDeacetylase activityBiochemistry
researchProduct

Characterization of pea histone deacetylases

1988

The present paper is the first report on histone deacetylases from plants. Three enzyme fractions with histone deacetylase activity (HD0, HD1 and HD2) have been partially purified from pea (Pisum sativum) embryonic axes. They deacetylate biologically acetylated chicken histones and, to a lesser extent, chemically acetylated histones, this being a criterion of their true histone deacetylase nature. The three enzymes are able to accept nucleosomes as substrates. HD1 is not inhibited by n-butyrate up to 50 mM, whereas HD0 and HD2 are only slightly inhibited, thereby establishing a clear difference to animal histone deacetylases. The three activities are inhibited by acetate, Cu(2+) and Zn(2+) …

Histone deacetylase 5Histone deacetylase 2HDAC11HDAC10Plant ScienceGeneral MedicineBiologySAP30BiochemistryHistone methyltransferaseGeneticsHistone deacetylase activityHistone deacetylaseAgronomy and Crop SciencePlant Molecular Biology
researchProduct