Core Insights - The research identifies a conserved mechanism for the formation of pericentric heterochromatin driven by H3K14ub-dependent SUV39H compartmentalization, revealing new insights into the mechanisms of heterochromatin formation, maintenance, and genetic stability in mammalian cells [3][7]. Group 1: Mechanism and Findings - The study discovered that G2E3 is a specific E3 ubiquitin ligase that recognizes H3K14ub, localized in pericentric heterochromatin regions, and enhances SUV39H-mediated H3K9me3, driving the localization of SUV39H and H3K9me3 in these regions [6][7]. - G2E3 is highly expressed during the G2/M phase and catalyzes H3K14ub, which lays the foundation for the sequential recruitment of SUV39H and HP1 proteins [7]. - The absence of G2E3 leads to the disruption of pericentric heterochromatin structure and abnormal accumulation of SUV39H and H3K9me3 in euchromatin regions, resulting in widespread transcriptional repression [7]. Group 2: Implications - The findings highlight the critical role of H3K14ub-dependent SUV39H compartmentalization in the correct partitioning of heterochromatin and euchromatin, as well as in the transcriptional regulation of euchromatin [7]. - This research addresses the molecular mechanisms underlying the formation and dynamic maintenance of mammalian heterochromatin, providing a new paradigm for epigenetic regulation [7].
华东师范大学发表最新Nature论文
生物世界·2025-10-16 00:00