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Niedner-Boblenz, Annika ; Monecke, Thomas ; Hennig, Janosch ; Klostermann, Melina ; Hofweber, Mario ; Davydova, Elena ; Gerber, André P. ; Anosova, Irina ; Mayer, Wieland ; Müller, Marisa ; Heym, Roland Gerhard ; Janowski, Robert ; Paillart, Jean-Christophe ; Dormann, Dorothee ; Zarnack, Kathi ; Sattler, Michael ; Niessing, Dierk:
Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation.
In: Nucleic Acids Research.
(2024)
.
- gkae1107.
ISSN 1362-4962
DOI: https://doi.org/10.1093/nar/gkae1107
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 membraneless organelles. The general function and wide distribution of PUN motifs across species suggest that in an ancient 'RNA world' PUN-like motifs may have supported the correct folding of early ribozymes.