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

• DOI: 10.1242/dev.175547
• Publication Date: 2019-06-12T18:49:00Z
• Authors: Xiukun Wang; Jun-Yan Kang; Leixin Wei; Xiaogan Yang; Hongduo Sun; Suming Yang; Lei Lu; Meng Yan; Meizhu Bai; Yanyan Chen; Juanjuan Long; Na Li; Dangsheng Li; Jing Huang; Ming Lei; Zhen Shao; Wen Yuan; Erwei Zuo; Kehuan Lu; Mo-Fang Liu; Jinsong Li
• Keywords: Spermiogenesis

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 exchange in mice. PHF7 specifically expressed during deletion results male infertility due to aberrant histone retention impaired protamine replacement elongated spermatids. Mechanistically, can simultaneously bind H2A H3; its domain, code reader, H3K4me3/me2 writer, ubiquitinate H2A. Thus, our study reveals novel E3 ligase through binding prior exchange.