Histone degradation by the proteasome regulates chromatin and cellular plasticity. (13th May 2021)

• Record Type: Journal Article
• Authors: Shmueli, Merav D.; Sheban, Daoud; Eisenberg‐Lerner, Avital; Merbl, Yifat
• Is Part Of: FEBS journal. Volume 289:Number 12(2022)
• Page Start: 3304
• Page End: 3316
• Publication Date: 2021-05-13
• Subjects: histone degradation -- histone modifications -- proteasome -- ubiquitin; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pathology, Molecular -- Periodicals; 572
• DOI: 10.1111/febs.15903
• Languages: English
• ISSNs: 1742-464X

Abstract

Abstract : Histones constitute the primary protein building blocks of the chromatin and play key roles in the dynamic control of chromatin compaction and epigenetic regulation. Histones are regulated by intricate mechanisms that alter their functionality and stability, thereby expanding the regulation of chromatin‐transacting processes. As such, histone degradation is tightly regulated to provide spatiotemporal control of cellular histone abundance. While several mechanisms have been implicated in controlling histone stability, here, we discuss proteasome‐dependent degradation of histones and the protein modifications that are associated with it. We then highlight specific cellular and physiological states that are associated with altered histone degradation by cellular proteasomes. Abstract : Histones constitute the primary protein building blocks of the chromatin and play key roles in the dynamic control of chromatin compaction and epigenetic regulation. Histone degradation is tightly regulated to provide spatiotemporal control of histone abundance and distribution over the chromatin. Here, we discuss mechanisms of proteasome‐dependent degradation of histones. We then highlight specific cellular and physiological states which are associated with altered histone degradation by proteasomes.