Ensemble structure of the N-terminal domain (1-267) of FUS in a biomolecular condensate.

ABSTRACT: Solutions of some proteins phase separate into a condensed state of high protein concentration and a dispersed state of low concentration. Such behavior is observed in living cells for a number of RNA-binding proteins that feature intrinsically disordered domains. It is relevant for cell function via the formation of membraneless organelles and transcriptional condensates. On a basic level, the process can be studied in vitro on protein domains that are necessary and sufficient for liquid-liquid phase separation (LLPS). We have performed distance distribution measurements by electron paramagnetic resonance for 13 sections in an N-terminal domain (NTD) construct of the protein fused in sarcoma (FUS), consisting of the QGSY-rich domain and the RGG1 domain, in the denatured, dispersed, and co

SUBMITTER: Esteban-Hofer L 

PROVIDER: S-EPMC10938082 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature