USP7 reduction leads to developmental failure of mouse early embryos

As a member of Ubiquitin-specific protease subfamily, ubiquitin specific protease 7 (USP7) has been reported to participate in a variety of cellular processes, including cell cycle, apoptosis, DNA damage response, and epigenetic modification. However, its function in preimplantation embryos is still obscure. To investigate the functions of USP7 during preimplantation embryo development, we used siRNA to degrade endogenous USP7 messenger RNA. We found that USP7 knockdown significantly decreased the development rate of mouse early embryos. Moreover, depletion of USP7 induced the accumulation of the DNA lesions and apoptotic blastomeres in early embryos. In addition, USP7 knockdown caused an abnormal H3K27me3 modification in 2-cell embryos. Overall, our results indicate that USP7 maintains genome stability perhaps via regulating H3K27me3 and DNA damage, consequently controlling the embryo quality.

Automated summary

As a member of Ubiquitin-specific protease subfamily, USP7 participates in a variety of cellular processes. However, its role in preimplantation embryos is unclear. Knockdown of USP7 decreased the development rate and induced DNA damage and apoptosis in early embryos. Furthermore, abnormal H3K27me3 modification was observed in 2-cell embryos with USP7 knockdown. Overall, USP7 plays a crucial role in maintaining genome stability and controlling embryo quality.