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尚无定论:新型翻译后修饰调控染色质功能

Nothing Is Yet Set in (Hi)stone: Novel Post-Translational Modifications Regulating Chromatin Function.

机构信息

Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.

Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.

出版信息

Trends Biochem Sci. 2020 Oct;45(10):829-844. doi: 10.1016/j.tibs.2020.05.009. Epub 2020 Jun 1.

DOI:10.1016/j.tibs.2020.05.009
PMID:32498971
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7502514/
Abstract

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.

摘要

组蛋白翻译后修饰 (PTMs) 已成为生物学调控的令人兴奋的机制,影响与癌症、免疫、大脑功能等相关的途径。仅在过去十年中,就发现了几种组蛋白 PTM,包括酰化、脂化、单胺化和糖化,其中许多似乎在核小体稳定性和转录调控中起着关键作用。在这篇综述中,我们讨论了过去 10 年内发现的新组蛋白 PTM,并特别关注修饰和加成的酶促与非酶促机制。此外,我们还考虑了这些新的组蛋白 PTM 如何适应所谓的“组蛋白密码”框架,强调这些 PTM 在代谢、发育和疾病状态中的生理相关性。

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