Hostname: page-component-7c8c6479df-ws8qp Total loading time: 0 Render date: 2024-03-19T07:24:27.596Z Has data issue: false hasContentIssue false

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Footnotes

*

These authors contributed equally to this work.

References

Akiyama, T, Kim, JM, Nagata, M and Aoki, F (2004). Regulation of histone acetylation during meiotic maturation in mouse oocytes. Mol Reprod Dev 69, 222–7.CrossRefGoogle ScholarPubMed
Ding, L, Pan, R, Huang, X, Wang, JX, Shen, YT, Xu, L, Zhang, Y, Liu, Y, He, XQ, Yang, XJ, Qi, ZQ and Wang, H (2012). Changes in histone acetylation during oocyte meiotic maturation in the diabetic mouse. Theriogenology 78, 784–92.CrossRefGoogle ScholarPubMed
Huang, X, Wang, HL, Qi, ST, Wang, ZB, Tong, JS, Zhang, QH, et al. (2011). DYNLT3 is required for chromosome alignment during mouse oocyte meiotic maturation. Reprod Sci 18, 983–9.CrossRefGoogle ScholarPubMed
Jenuwein, T and Allis, CD (2001). Translating the histone code. Science 293, 1074–80.CrossRefGoogle ScholarPubMed
Jin, L, Zhu, HY, Guo, Q, Li, XC, Zhang, YC, Zhang, GL, Xing, XX, Xuan, MF, Luo, QR, Yin, XJ and Kang, JD (2016). PCI-24781 can improve in vitro and in vivo developmental capacity of pig somatic cell nuclear transfer embryos. Biotechnol Lett 38, 1433–41.CrossRefGoogle ScholarPubMed
Kageyama, S, Liu, H, Kaneko, N, Ooga, M, Nagata, M and Aoki, F (2007). Alterations in epigenetic codifications during oocyte growth in mice. Reproduction 133, 8594.CrossRefGoogle Scholar
Kim, J-M, Ogura, A, Nagata, M and Aoki, F (2002). Analysis of the chromatin remodeling in the embryos reconstructed by somatic nuclear transfer. Biol Reprod 67, 760–6.CrossRefGoogle ScholarPubMed
Kruhlak, MJ, Hendzel, MJ, Fischle, W, Bertos, NR, Hameed, S, Yang, X-J, Verdin, E and Bazett-Jones, DP (2001). Regulation of global acetylation in mitosis through loss of histone acetyltransferases and deacetylases from chromatin. J Biol Chem 276, 38307–19.Google ScholarPubMed
Long, H, Lu, SS, Kuang, YP, Yan, ZG, Liang, HX, Yu, S, Chai, WR, Yan, Z and Lyu, QF (2013). Incubation of sperm heads impairs fertilization and early embryo development following intracytoplasmic sperm injection (ICSI) by decreasing oocyte activation in mice. Biotechnol Lett 35, 1823–9.CrossRefGoogle ScholarPubMed
Panero, J, Trelles, J, Rodano, V, Montserrat, JM, Iglesias, LE, Lewkowicz, ES and Iribarren, AM (2006). Microbial hydrolysis of acetylated nucleosides. Biotechnol Lett 28, 1077–81.CrossRefGoogle ScholarPubMed
Shahbazian, MD and Grunstein, M (2007). Functions of site-specific histone acetylation and deacetylation. Annu Rev Biochem 76, 75100.CrossRefGoogle ScholarPubMed
Sobajima, Aoki F and Kohmoto, K (1993). Activation of mitogen-activated protein kinase during meiotic maturation in mouse oocytes. J Reprod Fertil 97, 389–94.CrossRefGoogle ScholarPubMed
Zhang, YC, Jin, L, Zhu, HY, Guo, Q, Li, XC, Zhang, GL, Xing, XX, Xuan, MF, Luo, QR, Luo, ZB, Wang, JX, Cui, CD, Li, WX, Cui, ZY, Yin, XJ and Kang, JD (2017). The developmental competence of oocytes parthenogenetically activated by an electric pulse and anisomycin treatment. Biotechnol Lett 39, 189–96.CrossRefGoogle ScholarPubMed
Zuccotti, M, Piccinelli, A, Giorgi Rossi, P, Garagna, S and Redi, CA (1995). Chromatin organization during mouse oocyte growth. Mol Reprod Dev 41, 479–85.CrossRefGoogle ScholarPubMed