Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation.

ABSTRACT: RNA-binding proteins are essential for gene regulation and the spatial organization of cells. Here, we report that the yeast ribosome biogenesis factor Loc1p is an intrinsically disordered RNA-binding protein with eight repeating positively charged, unstructured nucleic acid binding (PUN) motifs. While a single of these previously undefined motifs stabilizes folded RNAs, multiple copies strongly cooperate to catalyze RNA folding. In the presence of RNA, these multivalent PUN motifs drive phase separation. Proteome-wide searches in pro- and eukaryotes for proteins with similar arrays of PUN motifs reveal a strong enrichment in RNA-mediated processes and DNA remodeling. Thus, PUN motifs are potentially involved in a large variety of RNA- and DNA-related processes by concentrating them in mem

SUBMITTER: Niedner-Boblenz A 

PROVIDER: S-EPMC11662656 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature