Asymmetric oligomerization state and sequence patterning can tune multiphase condensate miscibility.

ABSTRACT: Endogenous biomolecular condensates, composed of a multitude of proteins and RNAs, can organize into multiphasic structures with compositionally distinct phases. This multiphasic organization is generally understood to be critical for facilitating their proper biological function. However, the biophysical principles driving multiphase formation are not completely understood. Here we use in vivo condensate reconstitution experiments and coarse-grained molecular simulations to investigate how oligomerization and sequence interactions modulate multiphase organization in biomolecular condensates. We demonstrate that increasing the oligomerization state of an intrinsically disordered protein results in enhanced immiscibility and multiphase formation. Interestingly, we find that oligomerization

SUBMITTER: Rana U 

PROVIDER: S-EPMC11230906 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature