Evolution of CPEB4 Dynamics Across its Liquid-Liquid Phase Separation Transition.

ABSTRACT: Knowledge about the structural and dynamic properties of proteins that form membrane-less organelles in cells via liquid-liquid phase separation (LLPS) is required for understanding the process at a molecular level. We used spin labeling and electron paramagnetic resonance (EPR) spectroscopy to investigate the dynamic properties (rotational diffusion) of the low complexity N-terminal domain of cytoplasmic polyadenylation element binding-4 protein (CPEB4_NTD) across its LLPS transition, which takes place with increasing temperature. We report the coexistence of three spin labeled CPEB4_NTD (CPEB4*) populations with distinct dynamic properties representing different conformational spaces, both before and within the LLPS state. Monomeric CPEB4* exhibiting fast motion defin

SUBMITTER: Seal M 

PROVIDER: S-EPMC8647080 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature