BOLL-containing Aggregate Mediates Translational Regulation During Human Oogenesis

Human oocyte meiosis utilizes a specialized translational control strategy to coordinate meiotic progression, mediated through dynamic regulation of mRNA stores. While germ cell-specific RNA-binding proteins (RBPs) are known to orchestrate this post-transcriptional program, the mechanistic basis of RBP-mediated cell fate specification remains elusive. Here, we demonstrate that BOLL, a Deleted in Azoospermia (DAZ) family protein, forms protein aggregates during meiotic prophase to drive translational reprogramming in human oogenesis. We determined that BOLL enhance translation efficiency of cell cycle regulators, as demonstrated by integrative translatome-transcriptome analysis combined with RNA immunoprecipitation sequencing. We also revealed the functional interaction network of BOLL with core translation machinery components through its conserved DAZ containing domain. Crucially, we identified the SDS-resistant protein aggregates as BOLL structural signature in human oocyte-like cells, demonstrated by semi-denaturing electrophoretic analysis. These finding delineate a protein aggregate-mediated regulatory paradigm where BOLL aggregates exert spatiotemporal control over cell cycle related genes during the meiotic prophase of human oogenesis.