Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory.

ABSTRACT: Electrostatic interactions and charge balance are important for the formation of biomolecular condensates involving proteins and nucleic acids. However, a detailed, atomistic picture of the charge distribution around proteins during the phase-separation process is lacking. Here, we use solution NMR spectroscopy to measure residue-specific near-surface electrostatic potentials (ϕ_ENS) of the positively charged carboxyl-terminal intrinsically disordered 103 residues of CAPRIN1, an RNA-binding protein localized to membraneless organelles playing an important role in messenger RNA (mRNA) storage and translation. Measured ϕ_ENS values have been mapped along the adenosine triphosphate (ATP)-induced phase-separation trajectory. In the absence of ATP, ϕ

SUBMITTER: Toyama Y 

PROVIDER: S-EPMC9457416 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature