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Updated: Sep 30, 2025

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
Published on: September 30, 2016
The role of ATP in solubilizing RNA-binding protein fused in sarcoma
Hayato Aida1, Yasuteru Shigeta2, Ryuhei Harada2
1College of Biological Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan.
Abstract:
Intrinsically disordered protein (IDP) plays an important role in liquid-liquid phase separation (LLPS). RNA-binding protein fused in sarcoma (FUS) is a well-studied IDP that induces LLPS since its low-complexity core region (FUS-LC-core) is essential for droplet formation through contacts between FUS-LC-cores. Several experimental studies have reported that adenosine triphosphate (ATP) concentrations modulate LLPS-driven droplet formation through the dissolution of FUS. To elucidate the role of ATP in this dissolution, microsecond-order all-atom molecular dynamics (MD) simulations were performed for a crowded system of FUS-LC-cores in the presence of multiple ATP molecules. Our analysis revealed that the adenine group of ATP frequently contacted the FUS-LC-core, and the phosphoric acid group of ATP was exposed to the external solvent, which promoted both hydration and solubilization of FUS.
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