Phase separation of PGL-3 driven by structured domains that oligomerize and interact with RGG motifs

ABSTRACT: Phase separation (PS) of biomolecular condensates is often assumed to be driven by interactions involving nucleic acids and intrinsically disordered regions (IDRs) of proteins. PGL-3 is a component of P granules, biomolecular condensates in C. elegans, that contains two structured domains (D1-D2), an internal IDR, and a C-terminal IDR rich with RGG motifs. Theoretical and in vitro studies implicated the internal IDR and RGG motifs in driving PGL-3 PS via self-interactions and binding to RNA. Studies in cells, however, implicated the D1 and D2 domains. Here, we investigate the molecular basis of PGL-3 PS in vitro using microscopy, crosslinking mass spectrometry, and biophysical measurements. We find that D1-D2 forms oligomers and is necessary and sufficient for PS. The terminal RGG region i

SUBMITTER: Rimpei Kuroiwa 

PROVIDER: S-SCDT-10_1038-S44319-026-00730-7 | biostudies-other |

REPOSITORIES: biostudies-other