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Dynamic alterations in H4K12 acetylation during meiotic maturation and after parthenogenetic activation of mouse oocytes

Published online by Cambridge University Press:  23 July 2020

Ze Zhang
Affiliation:
College of Animal Science and Technology, Hebei Agricultural University, Baoding, Hebei Province, 071000China
Baobao Chen
Affiliation:
College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu Province, 210000China
Haoliang Cui
Affiliation:
College of Animal Science and Technology, Hebei Agricultural University, Baoding, Hebei Province, 071000China
Haixu Gao
Affiliation:
College of Animal Science and Technology, Hebei Agricultural University, Baoding, Hebei Province, 071000China
Ming Gao
Affiliation:
College of Animal Science and Technology, Hebei Agricultural University, Baoding, Hebei Province, 071000China
Chenyu Tao*
Affiliation:
College of Animal Science and Technology, Hebei Agricultural University, Baoding, Hebei Province, 071000China
*
Author for correspondence: Chenyu Tao. College of Animal Science and Technology, Hebei Agricultural University, Baoding, Hebei Province, 071000China. Tel: +86 312 7528359. E-mail: taochenyuty@163.com

Summary

The aim of the study was to investigate the continuous changing pattern of H4K12 acetylation, and the expression levels of histone acetyltransferases (HATs) and histone deacetyltransferases (HDACs) in mouse oocytes during meiosis and after parthenogenetic activation (PA). The immunofluorescence results showed hyperacetylation of lysine-12 on histone H4 (H4K12) in the germinal vesicle (GV) oocytes that then decreased during germinal vesicle breakdown (GVBD), and disappeared in metaphase II (MII). However, it reappeared in the early 1-cell embryos derived after 4 h of PA. The expression levels of some selected HATs and HDACs also validated the changing pattern of H4K12 acetylation during meiosis and PA. In conclusion, H4K12 is deacetylated in GVBD and MII, and re-hyperacetylated after PA.

Type
Research Article
Copyright
© Cambridge University Press 2020

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Footnotes

*

These authors contributed equally to this work.

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