Interaction hot spots for phase separation revealed by NMR studies of a CAPRIN1 condensed phase.

ABSTRACT: The role of biomolecular condensates in regulating biological function and the importance of dynamic interactions involving intrinsically disordered protein regions (IDRs) in their assembly are increasingly appreciated. While computational and theoretical approaches have provided significant insights into IDR phase behavior, establishing the critical interactions that govern condensation with atomic resolution through experiment is more difficult, given the lack of applicability of standard structural biological tools to study these highly dynamic large-scale associated states. NMR can be a valuable method, but the dynamic and viscous nature of condensed IDRs presents challenges. Using the C-terminal IDR (607 to 709) of CAPRIN1, an RNA-binding protein found in stress granules, P bodies, an

SUBMITTER: Kim TH 

PROVIDER: S-EPMC8201762 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature