[an error occurred while processing this directive]

Hereditas(Beijing) ›› 2019, Vol. 41 ›› Issue (4): 285-292.doi: 10.16288/j.yczz.18-272

• Review • Previous Articles     Next Articles

Histone H3K27me3 in the regulation of skeletal muscle development

Yanmin Gan1,Jian Zhou1,Rong Quan1,Linjun Hong1,Zicong Li1,Enqin Zheng1,Dewu Liu1,Zhenfang Wu1,2,Gengyuan Cai1,2(),Ting Gu1()   

  1. 1. National Engineering Research Center for Breeding Swine Industry, College of Animal Science, South China Agricultural University, Guangzhou 510642, China
    2. Guangdong Wens Foodstuff Group Co., Ltd, Xinxing 527439, China
  • Received:2018-09-27 Revised:2019-02-26 Online:2019-04-20 Published:2019-03-05
  • Contact: Cai Gengyuan,Gu Ting E-mail:cgy0415@163.com;tinggu@scau.edu.cn
  • Supported by:
    the National Natural Science Foundation of China(31802036);the Guangdong Provincial Natural Science Foundation of China(2017A030310001)

Abstract:

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