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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Genome-wide maps of histone H2A.Z and its chaperone.

ABSTRACT: We use ChIP-Seq technology to profile the occupancy of histone H2A.Z and its chaperone in HeLa cells genome wide to check if they are co-colocalized. H2A.Z is ChIPed by antibody and its chaperone is tagged by Flag and ChIPed by M2 beads against Flag. ChIPed fragments are sequenced by Illumina HiSeq 2000 platform.

ORGANISM(S): Homo sapiens

SUBMITTER: Zhuqiang Zhang

PROVIDER: E-GEOD-52371 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Genome-wide maps of histone H2A.Z and its chaperone.

Project description:We use ChIP-Seq technology to profile the occupancy of histone H2A.Z and its chaperone in HeLa cells genome wide to check if they are co-colocalized.

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The histone chaperone Anp32e regulates memory formation, transcription and dendritic morphogenesis by regulating steady-state H2A.Z binding in neurons

Project description:Rapid removal of the histone variant H2A.Z from neural chromatin is a key step in learning-induced gene expression and memory formation, but the molecular mechanisms underlying learning-induced H2A.Z removal are unknown. Anp32e was recently identified an H2A.Z-specific histone chaperone that removes H2A.Z from nucleosomes in dividing cells, but whether it plays a similar role in non-dividing neurons is unknown. Moreover, prior studies only investigated effects of Anp32e on H2A.Z binding under steady state-conditions, such that its effect on H2A.Z removal under stimulus-induced conditions is unknown. Here, we show that Anp32e regulates H2A.Z binding in neurons under steady-state conditions, but that stimulus-induced H2A.Z removal is largely independent of Anp32e. In assessing the functional consequences of Anp32e, we showed that its depletion leads to H2A.Z-dependent impairment in dendritic arborization in cultured hippocampal neurons, as well as impaired recall of contextual fear memory and transcriptional regulation. Together, these data indicate the Anp32E regulates behavioral and morphological outcomes by preventing H2A.Z accumulation in chromatin rather than by regulating activity-mediated H2A.Z dynamics.

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Epigenetically induced paucity of histone H2A.Z stabilizes fission yeast ectopic centromeres

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