This review discusses how biomolecular condensates enhance 3' end processing in pre-mRNA, suggesting a new perspective on RNA-protein interactions.
Biomolecular condensates are membraneless assemblies of proteins and nucleic acids, often formed through liquid-liquid phase separation. They selectively concentrate specific biomolecules and play essential roles in diverse cellular processes and diseases. This review discusses the emerging roles of biomolecular condensates in pre-mRNA 3' end processing, a critical step in mRNA biogenesis. 3' end processing factors are enriched in intrinsically disordered regions and undergo phase separation to form condensates that, in turn, fine-tune the efficiency and specificity of 3' end processing. Additionally, we describe how distinct 3' end processing pathways are spatially and functionally compartmentalized within nuclear biomolecular condensates, such as nuclear speckles and histone locus bodies. Finally, we propose that 3' end processing represents a promising experimental system to investigate fundamental principles underlying biomolecular condensate formation and function. This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein-RNA Recognition RNA Interactions with Proteins and Other Molecules > RNA-Protein Complexes RNA Interactions with Proteins and Other Molecules > Protein-RNA Interactions: Functional Implications.
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