Highly Charged Proteins and Their Repulsive Interactions Antagonize Biomolecular Condensation.

ABSTRACT: Biomolecular condensation is involved in various cellular processes; therefore, regulation of condensation is crucial to prevent deleterious protein aggregation and maintain a stable cellular environment. Recently, a class of highly charged proteins, known as heat-resistant obscure (Hero) proteins, was shown to protect other client proteins from pathological aggregation. However, the molecular mechanisms by which Hero proteins protect other proteins from aggregation remain unknown. In this study, we performed multiscale molecular dynamics (MD) simulations of Hero11, a Hero protein, and the C-terminal low-complexity domain (LCD) of the transactive response DNA-binding protein 43 (TDP-43), a client protein of Hero11, under various conditions to examine their interactions with each other. We

SUBMITTER: Tan C 

PROVIDER: S-EPMC10052238 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature