0000000000936478

AUTHOR

Giovanni Cenci

0000-0002-9628-1411

showing 2 related works from this author

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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A conserved role for the mitochondrial citrate transporter Sea/SLC25A1 in the maintenance of chromosome integrity.

2009

Histone acetylation plays essential roles in cell cycle progression, DNA repair, gene expression and silencing. Although the knowledge regarding the roles of acetylation of histone lysine residues is rapidly growing, very little is known about the biochemical pathways providing the nucleus with metabolites necessary for physiological chromatin acetylation. Here, we show that mutations in the scheggia (sea)-encoded Sea protein, the Drosophila ortholog of the human mitochondrial citrate carrier Solute carrier 25 A1 (SLC25A1), impair citrate transport from mitochondria to the cytosol. Interestingly, inhibition of sea expression results in extensive chromosome breakage in mitotic cells and indu…

MaleAnion Transport ProteinsBlotting WesternMolecular Sequence DataOrganic Anion Transporterscitrate transporterSAP30BiologyModels BiologicalHistonesMitochondrial ProteinsHistone H2AGeneticsHistone codeAnimalsDrosophila ProteinsHumansAmino Acid SequenceCitratesSLC25A1Molecular BiologyGenetics (clinical)Cells CulturedConserved SequenceChromosome Aberrationsmetabolism epigenetics histone acetylation AcCoA Citrate carrierSequence Homology Amino AcidChromosome integrityhistone acetylationHDAC8AcetylationChromosome BreakageGeneral MedicineCitrate transportFibroblastsHDAC4mitochondriaHistoneBiochemistryAcetylationMutationcitrate transporter histone acetylationbiology.proteinFemaleRNA InterferenceCarrier ProteinsHuman molecular genetics
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