Search results for "histone acetylation"

showing 9 items of 19 documents

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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Acetylated nucleosome assembly on telomeric DNAs

2003

Abstract The role of histone N-terminal domains on the thermodynamic stability of nucleosomes assembled on several different telomeric DNAs as well as on ‘average’ sequence DNA and on strong nucleosome positioning sequences, has been studied by competitive reconstitution. We find that histone tails hyperacetylation favors nucleosome formation, in a similar extent for all the examined sequences. On the contrary, removal of histone terminal domains by selective trypsinization causes a decrease of nucleosome stability which is smaller for telomeres compared to the other sequences examined, suggesting that telomeric sequences have only minor interactions with histone tails. Micrococcal nuclease…

Nucleosome assemblyBiophysicsBinding CompetitiveBiochemistryHistonesKluyveromycesHistone H1Histone methylationAnimalsHumansMicrococcal NucleaseNucleosomeHistone codeHistone octamerChemistrynucleosomeChlamydomonasOrganic Chemistryhistone acetylationhistone acetylation; nucleosome; nucleosome positioning; telomeres; thermodynamic stabilityAcetylationDNATelomeretelomeresLinker DNANucleosomesProtein Structure TertiaryBiochemistryChromatosomeBiophysicsthermodynamic stabilityThermodynamicsnucleosome positioningBiophysical Chemistry
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Interactions between polyamines, acetylpolyamines and PCAF during histone acetylation.

2009

Polyamines are involved in several gene regulatory functions, as the transcription process. In order to clarify their effect, in an initial “in vitro” biochemical study, we considered their influence on the nuclear PCAF acetyltransferase (PCAF-HAT). In a model system, using both commercial histones and laboratory histone preparations from mammary epithelial cells, we evidenced the inhibitory effect played by 40-180 uM spermidine (Spd) versus PCAF, assayed on 250 nM histone and 40 uM acetyl-CoA. At the same concentrations N8-acetylspermidine (N8-Ac.Spd), the acetylated form of spermidine located in the nucleus, exerts a significant activating effect on the PCAF-HAT. In addition, N8-Ac.Spd se…

PolyamineAcetylpolyamineHistone acetylation.Settore BIO/10 - BiochimicaHAT
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PCAF catalyzes tha acetylation of spermidine to N8-acetylspermidine and regulates its acetylating activity on histones

2011

Post-transcriptional histone acetylation is a well known process playing a crucial role in chromatin assembly and transcription. Here, we report that PCAF, a highly conserved histone acetyltransferase (HAT), can efficiently catalyze acetylation of spermidine to N8-acetylspermidine, at low concentration. Remarkably, we found that spermidine at higher concentration can also inhibit PCAF HAT activity directed against histone H3 in vitro, confirming the in vivo data referred by Eisenberg et al. on the spermidine induced inhibition of H3 acetylation. Surprisingly when we performed HAT assay experiments at low spermidine concentration we observed an activating effect on PCAF on H3 acetylation. Ou…

Settore BIO/10 - BiochimicaSpermidine PCAF Histone acetylation Spermidine acetylation
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Lifelong exposure to low dose xeno-hormones in rats : multi-generational effects of xeno-hormone mixtures on taste preferences, maternal behavior, an…

2012

During the last decade, the issue of health-related endocrine disruptors (ED) has been extended to the toxicity of mixtures. The objective of this study was to define the effects of lifelong exposure to ED mixtures, at low doses defined as "non-harmful" by the authorities. In this aim, the effects of mixtures combining genistein, vinclozolin and bisphenol A, have been investigated in the rat by using an integrative and multi-generational experimental approach which takes into account maternal behavior, feeding behavior and development. Our results show that these mixtures could: a) reduce maternal behavior, b) change taste preferences (sweet, salty), c) affect the development from the in ut…

Submandibular gland[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesDimorphisme sexuel[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyTolérance au glucoseXéno-hormonesXeno-hormonesAdipose tissueTissu adipeuxGlucose toleranceProtéines salivairesSalivary proteinsSexual dimorphismCholesterolCholestérolHistone acetylationGustineGlande submandibulaireAcétylation des histones
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The histone deacetylase Rpd3 regulates the heterochromatin structure of Drosophila telomeres

2011

Telomeres are specialized structures at the end of eukaryotic chromosomes that are required to preserve genome integrity, chromosome stability and nuclear architecture. Telomere maintenance and function are established epigenetically in several eukaryotes. However, the exact chromatin enzymatic modifications regulating telomere homeostasis are poorly understood. In Drosophila melanogaster, telomere length and stability are maintained through the retrotransposition of specialized telomeric sequences and by the specific loading of protecting capping proteins, respectively. Here, we show that the loss of the essential and evolutionarily conserved histone deacetylase Rpd3, the homolog of mammal…

Telomere-binding proteinGeneticsEpigenomicsMaleHistone deacetylase 5Histone deacetylase 2HDAC11Histone Deacetylase 1Cell BiologyBiologyTelomereHistone H4Telomere HomeostasisDrosophila melanogasterHeterochromatinHistone H2Ahistone deacetylaseHistone codeAnimalsDrosophila Proteinsanimals; article; chromosome aberration; chromosome structure; drosophila; drosophila melanogaster; drosophila proteins; enzyme activity; epigenetics; epigenomics; eukaryota; heterochromatin; histone acetylation; histone deacetylase 1; histone deacetylase rpd 3; histone methylation; male; mammalia; nonhuman; polytene chromosome; priority journal; regulatory mechanism; telomere; unclassified drugPolytene Chromosomes
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Tributyltin(Iv) butyrate: A novel epigenetic modifier with er stress-and apoptosis-inducing properties in colon cancer cells

2021

Organotin(IV) compounds are a class of non-platinum metallo-conjugates exhibiting antitumor activity. The effects of different organotin types has been related to several mechanisms, including their ability to modify acetylation protein status and to promote apoptosis. Here, we focus on triorganotin(IV) complexes of butyric acid, a well-known HDAC inhibitor with antitumor properties. The conjugated compounds were synthesized and characterised by FTIR spectroscopy, multi-nuclear (1H, 13C and 119Sn) NMR, and mass spectrometry (ESI-MS). In the triorganotin(IV) complexes, an anionic monodentate butyrate ligand was observed, which coordinated the tin atom on a tetra-coordinated, monomeric enviro…

Triorganotin(IV) butyratesPharmaceutical ScienceOrganic chemistryApoptosisButyrateArticleHistone DeacetylasesAnalytical ChemistryEpigenesis GeneticButyric acidchemistry.chemical_compoundQD241-441HDAC inhibitorsCell Line TumorSettore BIO/10 - BiochimicaDrug DiscoveryHumansPhysical and Theoretical ChemistrybiologyAcetylationLigand (biochemistry)Endoplasmic Reticulum StressColon cancerHistonechemistryBiochemistryHistone acetylationChemistry (miscellaneous)ApoptosisAcetylationSettore CHIM/03 - Chimica Generale E InorganicaColonic NeoplasmsTributyltinbiology.proteinUnfolded protein responseMolecular MedicineButyric AcidTrialkyltin CompoundsER stressProtein Processing Post-Translational
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Exposition continue aux xéno-hormones à faibles doses chez le rat : effets multi-générationnels de mélanges sur les préférences gustatives, le compor…

2012

During the last decade, the issue of health-related endocrine disruptors (ED) has been extended to the toxicity of mixtures. The objective of this study was to define the effects of lifelong exposure to ED mixtures, at low doses defined as "non-harmful" by the authorities. In this aim, the effects of mixtures combining genistein, vinclozolin and bisphenol A, have been investigated in the rat by using an integrative and multi-generational experimental approach which takes into account maternal behavior, feeding behavior and development. Our results show that these mixtures could: a) reduce maternal behavior, b) change taste preferences (sweet, salty), c) affect the development from the in ut…

XÉNO-HORMONES;DIMORPHISME SEXUEL;TISSU ADIPEUX;GLANDE SUBMANDIBULAIRE;PROTÉINES SALIVAIRES;GUSTINE;TOLÉRANCE AU GLUCOSE;CHOLESTÉROL;HISTONE ACÉTYLATION[SDV.AEN] Life Sciences [q-bio]/Food and NutritionXENO-HORMONES;SEXUAL DIMORPHISM;ADIPOSE TISSUE;SUBMANDIBULAR GLAND;SALIVARY PROTEINS;GUSTINE;GLUCOSE TOLERANCE;CHOLESTEROL;HISTONE ACETYLATION[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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On the ubiquitous presence of histone acetyltransferase B in eukaryotes

1985

AbstractHistone acetyltransferase B activity has been found in pea (Pisun sativum) seedlings. The enzyme has been partially purified and it has been found that it is highly specific for H4. The results confirm that histone acetyltransferase B occurs in 3 eukaryotic kingdoms.

educationBiophysicsBiochemistrySativumHistone H1Structural BiologyHistone H2AGeneticsMolecular BiologyPisum sativumchemistry.chemical_classificationbiologyfood and beveragesCell BiologyHistone acetyltransferaseChromatinhumanitiesChromatinHistone acetyltransferase BEnzymeHistone acetylationPCAFBiochemistrychemistryHistone methyltransferasebiology.proteinFEBS Letters
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