5w4d

Publication Abstract from PubMed

Cytoplasmic RNA-protein (RNP) granules have diverse biophysical properties, from liquid to solid, and play enigmatic roles in RNA metabolism. Nematode P granules are paradigmatic liquid droplet granules and central to germ cell development. Here we analyze a key P granule scaffolding protein, PGL-1, to investigate the functional relationship between P granule assembly and function. Using a protein-RNA tethering assay, we find that reporter mRNA expression is repressed when recruited to PGL-1. We determine the crystal structure of the PGL-1 N-terminal region to 1.5 A, discover its dimerization, and identify key residues at the dimer interface. Mutations of those interface residues prevent P granule assembly in vivo, de-repress PGL-1 tethered mRNA, and reduce fertility. Therefore, PGL-1 dimerization lies at the heart of both P granule assembly and function. Finally, we identify the P granule-associated Argonaute WAGO-1 as crucial for repression of PGL-1 tethered mRNA. We conclude that P granule function requires both assembly and localized regulators.

C. elegans germ granules require both assembly and localized regulators for mRNA repression.,Aoki ST, Lynch TR, Crittenden SL, Bingman CA, Wickens M, Kimble J Nat Commun. 2021 Feb 12;12(1):996. doi: 10.1038/s41467-021-21278-1. PMID:33579952^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.