组蛋白H3K27me3对骨骼肌发育调控研究进展
收稿日期: 2018-09-27
修回日期: 2019-02-26
网络出版日期: 2019-03-05
基金资助
国家自然科学基金项目(31802036);广东省自然科学基金项目(2017A030310001)
Histone H3K27me3 in the regulation of skeletal muscle development
Received date: 2018-09-27
Revised date: 2019-02-26
Online published: 2019-03-05
Supported by
the National Natural Science Foundation of China(31802036);the Guangdong Provincial Natural Science Foundation of China(2017A030310001)
组蛋白甲基化是发生在核小体核心组蛋白各亚基N-端肽链的一种修饰方式。在组成核小体的4种亚基中,H3亚基N-端肽链第4、9、27、36和79等位点的赖氨酸为甲基化热点,甲基化类型包括一、二、三甲基化(mono-, di-, tri-methylation)。H3K27me3是发生在组蛋白H3亚基第27位赖氨酸的三甲基化,主要发挥转录抑制的作用,参与骨骼肌的发育调控。研究表明,H3K27me3能够与骨骼肌增殖和分化的关键转录因子(如MyoD和MyoG等)及细胞周期蛋白特异性结合,并与其他表观遗传调控因子lncRNA及miRNA等互作,对骨骼肌的增殖和分化时间以及程度进行精细调控。本文系统介绍了组蛋白甲基化的类型以及H3K27甲基化和去甲基化的生物学过程,总结了目前已报道的H3K27me3在骨骼肌成肌细胞增殖和分化过程中发挥的作用,以期辅助科研工作者了解H3K27me3在骨骼肌发育过程中的作用,以及为进一步提高哺乳动物肌肉品质提供参考。
甘炎民,周健,全绒,洪林君,李紫聪,郑恩琴,刘德武,吴珍芳,蔡更元,顾婷 . 组蛋白H3K27me3对骨骼肌发育调控研究进展[J]. 遗传, 2019 , 41(4) : 285 -292 . DOI: 10.16288/j.yczz.18-272
Histone methylation is a modification which occurs in the N-terminal peptide chains of the histone nucleosome. The 4th, 9th, 27th, 36th and 79th lysines in N-terminal peptide chain of histone H3 are hot spots for this modification, including mono-, di-, and tri-methylation. H3K27me3 is the tri-methylation modification on histone H3 lysine 27, which mainly functions as a transcriptional repressor regulating skeletal muscle development. Studies have shown that H3K27me3 can finely regulate skeletal muscle proliferation, including the level and duration of skeletal muscle development by specifically binding to myogenic regulatory factors (e.g., MyoD, MyoG, etc.), cell cycling regulators, and epigenetic regulators including lncRNA and miRNA. In this review, we introduce the types and mechanisms of histone methylation and de-methylation of H3K27. We also summarize how H3K27me3 functions in the proliferation and differentiation of skeletal muscle cell. This review will contribute to the comprehension of the function of H3K27me3 in regulating skeletal muscle development and provide reference for further improving our understanding of mammalian muscle.
Key words: histone; methylation; skeletal muscle; H3K27me3
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