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PHF7 is a novel histone H2A E3 ligase prior to histone-to-protamine exchange during spermiogenesis.

Abstract

Epigenetic regulation, including histone-to-protamine exchanges, controls spermiogenesis. However, the underlying mechanisms of this regulation are largely unknown. Here, we report that PHF7, a testis-specific PHD and RING finger domain-containing protein, is essential for histone-to-protamine exchange in mice. PHF7 is specifically expressed during spermiogenesis. PHF7 deletion results in male infertility due to aberrant histone retention and impaired protamine replacement in elongated spermatids. Mechanistically, PHF7 can simultaneously bind histone H2A and H3; its PHD domain, a histone code reader, can specifically bind H3K4me3/me2, and its RING domain, a histone writer, can ubiquitylate H2A. Thus, our study reveals that PHF7 is a novel E3 ligase that can specifically ubiquitylate H2A through binding H3K4me3/me2 prior to histone-to-protamine exchange.

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  • Authors+Show Affiliations

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    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China.

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    State Key Laboratory of Molecular Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China.

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    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China. Department of Orthopaedic Surgery, Changzheng Hospital, The Second Military Medical University, Shanghai 200003, China.

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    State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, Animal Reproduction Institute, Guangxi University, Nanning, Guangxi 530004, China.

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    Key Laboratory of Computational Biology, CAS-MPG Partner Institute for Computational Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.

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    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China.

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    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China.

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    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China.

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    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China.

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    National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 333 Haike Road, Shanghai 201203, China.

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    National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 333 Haike Road, Shanghai 201203, China.

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    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China.

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    CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, Shanghai 200031, China.

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    National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 333 Haike Road, Shanghai 201203, China.

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    National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 333 Haike Road, Shanghai 201203, China.

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    Key Laboratory of Computational Biology, CAS-MPG Partner Institute for Computational Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.

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    Department of Orthopaedic Surgery, Changzheng Hospital, The Second Military Medical University, Shanghai 200003, China jsli@sibcb.ac.cn mfliu@sibcb.ac.cn kehuanlu@163.com erweizuo@163.com yuanwenspine@163.com.

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    State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, Animal Reproduction Institute, Guangxi University, Nanning, Guangxi 530004, China jsli@sibcb.ac.cn mfliu@sibcb.ac.cn kehuanlu@163.com erweizuo@163.com yuanwenspine@163.com. Research Center of Animal Genomics, Agricultural Genomics Institute at Shengzhen, Chinese Academy of Agricultural Sciences, Shengzhen, Guangdong 518210, China.

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    State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, Animal Reproduction Institute, Guangxi University, Nanning, Guangxi 530004, China jsli@sibcb.ac.cn mfliu@sibcb.ac.cn kehuanlu@163.com erweizuo@163.com yuanwenspine@163.com.

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    State Key Laboratory of Molecular Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China jsli@sibcb.ac.cn mfliu@sibcb.ac.cn kehuanlu@163.com erweizuo@163.com yuanwenspine@163.com.

    State Key Laboratory of Cell Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Chinese Academy of Science, University of Chinese Academy of Science, Shanghai 200031, China jsli@sibcb.ac.cn mfliu@sibcb.ac.cn kehuanlu@163.com erweizuo@163.com yuanwenspine@163.com.

    Source

    Development (Cambridge, England) 146:13 2019 Jul 10 pg

    Pub Type(s)

    Journal Article

    Language

    eng

    PubMed ID

    31189663

    Citation

    Wang, Xiukun, et al. "PHF7 Is a Novel Histone H2A E3 Ligase Prior to Histone-to-protamine Exchange During Spermiogenesis." Development (Cambridge, England), vol. 146, no. 13, 2019.
    Wang X, Kang JY, Wei L, et al. PHF7 is a novel histone H2A E3 ligase prior to histone-to-protamine exchange during spermiogenesis. Development. 2019;146(13).
    Wang, X., Kang, J. Y., Wei, L., Yang, X., Sun, H., Yang, S., ... Li, J. (2019). PHF7 is a novel histone H2A E3 ligase prior to histone-to-protamine exchange during spermiogenesis. Development (Cambridge, England), 146(13), doi:10.1242/dev.175547.
    Wang X, et al. PHF7 Is a Novel Histone H2A E3 Ligase Prior to Histone-to-protamine Exchange During Spermiogenesis. Development. 2019 Jul 10;146(13) PubMed PMID: 31189663.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - PHF7 is a novel histone H2A E3 ligase prior to histone-to-protamine exchange during spermiogenesis. AU - Wang,Xiukun, AU - Kang,Jun-Yan, AU - Wei,Leixin, AU - Yang,Xiaogan, AU - Sun,Hongduo, AU - Yang,Suming, AU - Lu,Lei, AU - Yan,Meng, AU - Bai,Meizhu, AU - Chen,Yanyan, AU - Long,Juanjuan, AU - Li,Na, AU - Li,Dangsheng, AU - Huang,Jing, AU - Lei,Ming, AU - Shao,Zhen, AU - Yuan,Wen, AU - Zuo,Erwei, AU - Lu,Kehuan, AU - Liu,Mo-Fang, AU - Li,Jinsong, Y1 - 2019/07/10/ PY - 2019/01/09/received PY - 2019/05/28/accepted PY - 2019/6/14/pubmed PY - 2019/6/14/medline PY - 2019/6/14/entrez KW - E3 ligase KW - Histone H2A ubiquitylation KW - Histone-to-protamine exchange KW - PHF7 KW - Spermiogenesis JF - Development (Cambridge, England) JO - Development VL - 146 IS - 13 N2 - Epigenetic regulation, including histone-to-protamine exchanges, controls spermiogenesis. However, the underlying mechanisms of this regulation are largely unknown. Here, we report that PHF7, a testis-specific PHD and RING finger domain-containing protein, is essential for histone-to-protamine exchange in mice. PHF7 is specifically expressed during spermiogenesis. PHF7 deletion results in male infertility due to aberrant histone retention and impaired protamine replacement in elongated spermatids. Mechanistically, PHF7 can simultaneously bind histone H2A and H3; its PHD domain, a histone code reader, can specifically bind H3K4me3/me2, and its RING domain, a histone writer, can ubiquitylate H2A. Thus, our study reveals that PHF7 is a novel E3 ligase that can specifically ubiquitylate H2A through binding H3K4me3/me2 prior to histone-to-protamine exchange. SN - 1477-9129 UR - https://www.unboundmedicine.com/medline/citation/31189663/PHF7_is_a_novel_histone_H2A_E3_ligase_prior_to_histone-to-protamine_exchange_during_spermiogenesis L2 - http://dev.biologists.org/cgi/pmidlookup?view=long&pmid=31189663 DB - PRIME DP - Unbound Medicine ER -