期刊
BIOLOGY OF REPRODUCTION
卷 81, 期 4, 页码 739-748出版社
SOC STUDY REPRODUCTION
DOI: 10.1095/biolreprod.109.076497
关键词
CDC2/cyclin B1; cell cycle; HSPA2; linker histones; meiosis; NASP; spermatogenesis; synamptonemal complex; testis
资金
- Eunice Kennedy Shriver National Institute of Child Health
- Human Development/National Institutes of Health [U54 (HD35041)]
In mammalian spermatocytes, cell division cycle protein 2 (CDC2)/cyclin B1 and the chaperone heat shock protein A2 (HSPA2) are required for the G2 -> M transition in prophase I. Here, we demonstrate that in primary spermatocytes, linker histone chaperone testis/embryo form of nuclear autoantigenic sperm protein (tNASP) binds the heat shock protein HSPA2, which localizes on the synaptonemal complex of spermatocytes. Significantly, the tNASP-HSPA2 complex binds linker histones and CDC2, forming a larger complex. We demonstrate that increasing amounts of tNASP favor tNASP-HSPA2-CDC2 complex formation. Binding of linker histones to tNASP significantly increases HSPA2 ATPase activity and the capacity of tNASP to bind HSPA2 and CDC2, precluding CDC2/cyclin B1 complex formation and, consequently, decreasing CDC2/cyclin B1 kinase activity. Linker histone binding to NASP controls the ability of HSPA2 to activate CDC2 for CDC2/cyclin B1 complex formation; therefore, tNASP's role is to provide the functional link between linker histones and cell cycle progression during meiosis.
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