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GenomicsGenome-wide incorporation dynamics reveal distinct categories of turnover for the histone variant H3.3
We developed a system to study the DNA replication-independent turnover nucleosomes containing the histone variant H3.3 in mammalian cells. By measuring the genome-wide incorporation of H3.3 at different time points following epitope-tagged H3.3 expression, we find three categories of H3.3-nucleosom...
ORGANISM(S): Mus musculus 
2013-10-23 | E-GEOD-51505 | biostudies-arrayexpress
GenomicsHistone turnover during DNA replication
Histone turnover during DNA replication
PRJNA794181 | ENA
TranscriptomicsExpression profiles of the NuB4/HAT-B complex and histone knockouts
Dynamic modification of histone proteins plays a key role in regulating gene expression. However, histones themselves can also be dynamic, which potentially affects the stability of histone modifications. To determine the molecular mechanisms of histone turnover we developed a parallel screening met...
ORGANISM(S): Saccharomyces cerevisiae 
2012-05-14 | E-GEOD-30168 | biostudies-arrayexpress
TranscriptomicsCATCH-IT method for measuring nucleosome turnover
Direct measurement of nucleosome turnover dynamics by using co-translational incorporation of the methionine (Met) surrogate azidohomoalaine (Aha) into proteins and subsequent ligation of biotin to Aha-containing proteins through the [3+2] cycloaddition reaction between the azide group of Aha and an...
ORGANISM(S): Drosophila melanogaster 
2010-05-27 | E-GEOD-19788 | biostudies-arrayexpress
TranscriptomicsHistone H1 binding is restricted by histone variant H3.3 (DamID)
Linker histones are involved in the formation of higher-order chromatin structure. Although linker histones have been implicated in the regulation of specific genes, it still remains unclear what their principal binding determinants are and how their repressive function in vitro can be reconciled wi...
ORGANISM(S): Drosophila melanogaster 
2010-06-21 | E-GEOD-16883 | biostudies-arrayexpress
ProteomicsQuantifying histone PTMs by bottom-up MS
Histone post-translational modifications (PTMs) contribute to chromatin function through their chemical properties which influence chromatin structure, and their ability to recruit chromatin interacting proteins. Nanoflow liquid chromatography coupled with high resolution tandem mass spectrometry (n...
ORGANISM(S): Homo sapiens (Human) 
2015-03-27 | PXD001541 | Pride
Proteomics Post-translational modification Isobaric peptide Retention time Histone Quantification 
GenomicsDistribution of active (H3K4me1, H3K4me3, H3K27ac) and inactive (H3K9me3, H3K27me3) histone PTMs in WT and HIRA KO HeLa cells
We profiled the enrichment of active (H3K4me1, H3K4me3, H3K27ac) and inactive (H3K9me3, H3K27me3) histone PTMs in cells that are wild-type (WT) or knock-out (KO) for the H3.3-specific chaperone HIRA. We performed native ChIP-seq following MNase digestion to isolate nucleosomes in H3.1-SNAP and H3.3-...
ORGANISM(S): Homo sapiens 
2025-08-07 | E-MTAB-14416 | biostudies-arrayexpress
GenomicsNASP modulates histone turnover to drive PARP inhibitor resistance
NASP modulates histone turnover to drive PARP inhibitor resistance
PRJEB86492 | ENA
GenomicsCritical role of histone turnover in neuronal transcription and plasticity [ChIP-seq]
Turnover and exchange of nucleosomal histones and their variants, a process long believed to be static in post-replicative cells, remains largely unexplored in brain. Here, we describe a novel mechanistic role for HIRA (histone cell cycle regulator) and proteasomal degradation associated histone dyn...
ORGANISM(S): Mus musculus 
2015-06-23 | E-GEOD-69806 | biostudies-arrayexpress
TranscriptomicsHistone H1 binding is restricted by histone variant H3.3 (Nucleosome)
Linker histones are involved in the formation of higher-order chromatin structure. Although linker histones have been implicated in the regulation of specific genes, it still remains unclear what their principal binding determinants are and how their repressive function in vitro can be reconciled wi...
ORGANISM(S): Drosophila melanogaster 
2010-06-23 | E-GEOD-16882 | biostudies-arrayexpress
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