Apr 30, 2020

Proteasome activator PA200 maintains stability of histone marks during transcription and aging

BioRxiv : the Preprint Server for Biology
T. JiangXiaobo Qiu

Abstract

The epigenetic inheritance relies on stability of histone marks, but various diseases, including aging-related diseases, are usually associated with alterations of histone marks. How the stability of histone marks is maintained still remains unclear. The core histones can be degraded by the atypical proteasome, which contains the proteasome activator PA200, in an acetylation-dependent manner during somatic DNA damage response and spermiogenesis. Here we show that PA200 promotes the transcription-coupled degradation of the core histones, and plays an important role in maintaining the stability of histone marks. Degradation of the histone variant H3.3, which is incorporated into chromatin during transcription, was much faster than that of its canonical form H3.1, which is incorporated during DNA replication. This degradation of the core histones could be suppressed by the transcription inhibitor, the proteasome inhibitor or deletion of PA200. The histone deacetylase inhibitor accelerated the degradation rates of H3 in general, especially its variant H3.3, while the mutations of the putative acetyl-lysine-binding region of PA200 abolished histone degradation in the G1-arrested cells, supporting that acetylation is involved in the ...Continue Reading

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Mentioned in this Paper

Electronic Health Records
PubMed
Biomedical Ontologies
Nucleotide Excision Repair
Pharmacologic Substance
Naming, Function
Recognition (Psychology)
Biomedicine
United States National Institutes of Health

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