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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 ubiquitinate H2A. Thus, our study reveals that PHF7 is a novel E3 ligase that can specifically ubiquitinate H2A through binding H3K4me3\/me2 prior to histone-to-protamine exchange.<\/jats:p>","DOI":"10.1242\/dev.175547","type":"journal-article","created":{"date-parts":[[2019,6,12]],"date-time":"2019-06-12T18:49:00Z","timestamp":1560365340000},"source":"Crossref","is-referenced-by-count":39,"title":["PHF7 is a novel histone H2A E3 ligase prior to histone-to-protamine exchange during spermiogenesis"],"prefix":"10.1242","author":[{"given":"Xiukun","family":"Wang","sequence":"first","affiliation":[{"name":"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, 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