Significance The surface charges of biomolecules can significantly affect how they interact with each other, including, in some cases, whether they can undergo phase separation. One example is the RNA-binding… Click to show full abstract
Significance The surface charges of biomolecules can significantly affect how they interact with each other, including, in some cases, whether they can undergo phase separation. One example is the RNA-binding protein CAPRIN1, an important component in membraneless organelles involved in RNA processing. Focusing on the C-terminal intrinsically disordered, positively charged region of CAPRIN1, we have mapped at a residue-specific level the role of electrostatics in phase separation promoted by the addition of adenosine triphosphate. We show that the propensity of CAPRIN1 to form condensates is coupled to its neutralization and formation of intermolecular contacts. Our results highlight the interplay between repulsive electrostatic forces and favorable interchain interactions in regulating the formation of CAPRIN1 condensates.
               
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