Open AccessPHF7 is a novel histone H2A E3 ligase prior to histone-to-protamine exchange during spermiogenesis
Author(s) -
Xiukun Wang,
Jun-Yan Kang,
Leixin Wei,
Xiaogan Yang,
Hongduo Sun,
Suming Yang,
Lei Lü,
Meng Yan,
Meizhu Bai,
Yanyan Chen,
Juanjuan Long,
Na Li,
Dangsheng Li,
Jing Huang,
Ming Lei,
Zongping Shao,
Yan Wen,
Erwei Zuo,
LU Ke-huan,
Li Lin,
Jinsong Li
Publication year - 2019
Publication title -
development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.754
H-Index - 325
eISSN - 1477-9129
pISSN - 0950-1991
DOI - 10.1242/dev.175547
Subject(s) - biology , h3k4me3 , protamine , histone , spermiogenesis , histone h2a , histone methyltransferase , histone methylation , histone h3 , histone code , histone h4 , microbiology and biotechnology , genetics , biochemistry , sperm , dna , dna methylation , gene expression , gene , promoter , nucleosome , heparin
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 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.