0000000000063979

AUTHOR

Elena I. Georgieva

showing 5 related works from this author

Mobility of Acetylated Histones in Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis

1999

Abstract We describe an altered mobility for acetylated histone isoforms in sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Isoforms of histones H3 and H4 with a higher acetylation degree have a slightly faster electrophoretic mobility. Since acetylation neutralizes the positive charge of the e-amino group of lysine, without significantly changing the molecular mass of the protein, the acetylation-dependent mobility shift could be explained by the increase of the net negative charge of the SDS–histone complexes. A possible consequence of this differential mobility for the acetylation site determination by protein microsequencing from SDS gels is discussed.

ErythrocytesSodiumLysineBiophysicschemistry.chemical_elementBiochemistryHistoneschemistry.chemical_compoundElectrochemistryAnimalsSodium dodecyl sulfateMolecular BiologyPolyacrylamide gel electrophoresisGel electrophoresisChromatographyMolecular massReproducibility of ResultsSodium Dodecyl SulfateAcetylationCell BiologyBlood Protein ElectrophoresisElectrophoresischemistryBiochemistryAcetylationElectrophoresis Polyacrylamide GelChickensAnalytical Biochemistry
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Nucleosome-specific, Time-dependent Changes in Histone Modifications during Activation of the Early Growth Response 1 (Egr1) Gene

2014

Histone post-translational modifications and nucleosome remodeling are coordinate events involved in eukaryotic transcriptional regulation. There are relatively few data on the time course with which these events occur in individual nucleosomes. As a contribution to fill this gap, we first describe the nature and time course of structural changes in the nucleosomes -2, -1, and +1 of the murine Egr1 gene upon induction. To initiate the transient activation of the gene, we used the stimulation of MLP29 cells with phorbol esters and the in vivo activation after partial hepatectomy. In both models, nucleosomes -1 and +1 are partially evicted, whereas nucleosomes +1 and -2 slide downstream durin…

Time FactorsTranscription GeneticBiologyBiochemistryChromatin remodelingCell LineHistonesMiceHistone H1Histone methylationAnimalsHepatectomyHistone codeNucleosomeGene RegulationPromoter Regions GeneticMolecular BiologyEarly Growth Response Protein 1Mice KnockoutCell BiologyMolecular biologySWI/SNFLiver RegenerationNucleosomesCell biologyHistoneLiverChromatosomeHepatocytesbiology.proteinTetradecanoylphorbol AcetateProtein Processing Post-TranslationalJournal of Biological Chemistry
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A short-range gradient of histone H3 acetylation and Tup1p redistribution at the promoter of the Saccharomyces cerevisiae SUC2 gene.

2003

Chromatin immunoprecipitation assays are used to map H3 and H4 acetylation over the promoter nucleosomes and the coding region of the Saccharomyces cerevisiae SUC2 gene, under repressed and derepressed conditions, using wild type and mutant strains. In wild type cells, a high level of H3 acetylation at the distal end of the promoter drops sharply toward the proximal nucleosome that covers the TATA box, a gradient that become even steeper on derepression. In contrast, substantial H4 acetylation shows no such gradient and extends into the coding region. Overall levels of both H3 and H4 acetylation rise on derepression. Mutation of GCN5 or SNF2 lead to substantially reduced SUC2 expression; in…

Saccharomyces cerevisiae ProteinsTATA boxMutantGene ExpressionSaccharomyces cerevisiaeBiologyBiochemistryPolymerase Chain ReactionHistonesNucleosomeRNA MessengerHistone H3 acetylationDNA FungalPromoter Regions GeneticMolecular BiologyDerepressionHistone AcetyltransferasesAdenosine Triphosphatasesbeta-FructofuranosidaseWild typeChromosome MappingNuclear ProteinsCell BiologyMolecular biologyDNA-Binding ProteinsRepressor ProteinsAcetylationMutagenesisChromatin immunoprecipitationProtein KinasesTranscription FactorsThe Journal of biological chemistry
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Histone deacetylase A key enzyme for the binding of regulatory proteins to chromatin

1993

AbstractCore histones can be modified by reversible, posttranslational acetylation of specific lysine residues within the N-terminal protein domains. The dynamic equilibrium of acetylation is maintained by two enzyme activities, histone acetyltransferase and histone deacetylase. Recent data on histone deacetylases and on anionic motifs in chromatin- or DNA-binding regulatory proteins (e.g. transcription factors, nuclear proto-oncogenes) are summarized and united into a hypothesis which attributes a key function to histone deacetylation for the binding of regulatory proteins to chromatin by a transient, specific local increase of the positive charge in the N-terminal domains of nucleosomal c…

Models MolecularBiophysicsBiologyBiochemistryHistone DeacetylasesHistonesHistone H1Structural BiologyHistone H2AHistone methylationGeneticsAnimalsHumansHistone codeHistone octamerHistone deacetylaseMolecular BiologyOncogene proteinHistone deacetylase 2Cell BiologyMolecular biologyChromatinCell biologyHistone acetylationHistone methyltransferaseHistone deacetylaseTranscription factorTranscriptionProtein BindingTranscription FactorsFEBS Letters
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Transcription of the MAT2A gene, coding for methionine adenosyltransferase, is up-regulated by E2F and Sp1 at a chromatin level during proliferation …

2006

Methionine adenosyltransferase (MAT) is an essential enzyme because it catalyzes the formation of S-adenosylmethionine, the main methyl donor. Two MAT-encoding genes (MAT1A, MAT2A) are found in mammals. The latter is expressed in proliferating liver, dedifferentiation and cancer, whereas MAT1A is expressed in adult quiescent hepatocytes. Here, we report studies on the molecular mechanisms controlling the induction of MAT2A in regenerating rat liver and in proliferating hepatocytes. The MAT2A is up-regulated at two discrete moments during liver regeneration, as confirmed by RNApol-ChIP analysis. The first one coincides with hepatocyte priming (i.e. G0-G1 transition), while the second one tak…

MaleChromatin ImmunoprecipitationTranscription GeneticSp1 Transcription FactorMolecular Sequence DataOligonucleotidesElectrophoretic Mobility Shift AssayBiologyBiochemistryS PhaseSequence Homology Nucleic AcidmedicineAnimalsE2F1Electrophoretic mobility shift assayRats WistarPromoter Regions GeneticE2FE2F4Cells CulturedCell ProliferationSp1 transcription factorBase SequenceG1 PhaseMethionine AdenosyltransferaseCell BiologyMolecular biologyChromatinLiver regenerationE2F Transcription FactorsLiver RegenerationRatsUp-Regulationmedicine.anatomical_structureLiverMethionine AdenosyltransferaseHepatocyteHepatocytesProtein BindingThe International Journal of Biochemistry & Cell Biology
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