Acute Stress Induced Increase in Histone H3 Lys 9 Trimetylation in Rat Hippocampus
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ABSTRACT:
ORGANISM(S): Rattus norvegicus
PROVIDER: GSE41217 | GEO | 2012/11/02
SECONDARY ACCESSION(S): PRJNA176195
REPOSITORIES: GEO
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Project description:We utilized ChIP Seq to examine the the genomic localization of the increase in H3K9 trimethylation we had previously observed in the hippocampus as a consequence of acute restraint stress in rats (Hunter et. al PNAS 2009). Rats were restrained for 30 minutes, allowed to recover for 1 hour and then sacrificed and their hippocampi extracted and processed for H3K9me3 ChIP using the Cell Signalling H3K9me3 antibody.
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Project description:Histones modulate gene expression by chromatin compaction, regulating numerous processes such as differentiation. However, the mechanisms underlying histone degradation remain elusive. When compared with their differentiated counterparts, immortal human embryonic stem cells (hESCs) have a unique chromatin architecture and low levels of trimethylated histone H3 at lysine 9 (H3K9me3), a heterochromatin-associated modification. Here we assess a link between the intrinsic epigenetic landscape and ubiquitin-proteasome system of hESCs. We find that hESCs exhibit high expression of UBE2K, a ubiquitin-conjugating enzyme. Loss of UBE2K increases the levels of H3K9 trimethyltransferase SETDB1, resulting in H3K9 trimethylation and repression of neurogenic genes during differentiation. Concomitantly, loss of UBE2K impairs the ability of hESCs to differentiate into neural progenitors with neurogenic properties. Besides H3K9 trimethylation, we find that UBE2K binds histone H3 to induce its polyubiquitination and degradation by the proteasome. Notably, ubc-20, the worm orthologue of UBE2K, also regulates both histone H3 levels and H3K9 trimethylation in C. elegans germline. Thus, our results indicate that UBE2K crosses evolutionary boundaries to promote histone H3 degradation and reduce H3K9me3 repressive marks in immortal cells.
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