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Nothing Is Yet Set in (Hi)stone: Novel Post-Translational Modifications Regulating Chromatin Function.
Trends in Biochemical Sciences ( IF 11.6 ) Pub Date : 2020-06-01 , DOI: 10.1016/j.tibs.2020.05.009
Jennifer C Chan 1 , Ian Maze 2
Affiliation  

Histone post-translational modifications (PTMs) have emerged as exciting mechanisms of biological regulation, impacting pathways related to cancer, immunity, brain function, and more. Over the past decade alone, several histone PTMs have been discovered, including acylation, lipidation, monoaminylation, and glycation, many of which appear to have crucial roles in nucleosome stability and transcriptional regulation. In this review, we discuss novel histone PTMs identified within the past 10 years, with an extended focus on enzymatic versus nonenzymatic mechanisms underlying modification and adduction. Furthermore, we consider how these novel histone PTMs might fit within the framework of a so-called ‘histone code’, emphasizing the physiological relevance of these PTMs in metabolism, development, and disease states.



中文翻译:


(Hi)stone 尚未确定:调节染色质功能的新型翻译后修饰。



组蛋白翻译后修饰 (PTM) 已成为令人兴奋的生物调节机制,影响与癌症、免疫、脑功能等相关的通路。仅在过去十年中,就已经发现了多种组蛋白翻译后修饰,包括酰化、脂化、单氨酰化和糖化,其中许多似乎在核小体稳定性和转录调控中发挥着至关重要的作用。在这篇综述中,我们讨论了过去 10 年来发现的新型组蛋白 PTM,重点关注修饰和内合背后的酶促机制与非酶促机制。此外,我们考虑这些新颖的组蛋白 PTM 如何适应所谓的“组蛋白密码”的框架,强调这些 PTM 在代谢、发育和疾病状态中的生理相关性。

更新日期:2020-06-01
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