RG/RGG repeats in the C. elegans homologs of Nucleolin and GAR1 contribute to sub-nucleolar phase separation

Emily L. Spaulding (), Alexis M. Feidler, Lio A. Cook and Dustin L. Updike
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Emily L. Spaulding: The Mount Desert Island Biological Laboratory
Alexis M. Feidler: The Mount Desert Island Biological Laboratory
Lio A. Cook: The Mount Desert Island Biological Laboratory
Dustin L. Updike: The Mount Desert Island Biological Laboratory

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract The intrinsically disordered RG/RGG repeat domain is found in several nucleolar and P-granule proteins, but how it influences their phase separation into biomolecular condensates is unclear. We survey all RG/RGG repeats in C. elegans and uncover nucleolar and P-granule-specific RG/RGG motifs. An uncharacterized protein, K07H8.10, contains the longest nucleolar-like RG/RGG domain in C. elegans. Domain and sequence similarity, as well as nucleolar localization, reveals K07H8.10 (NUCL-1) to be the homolog of Nucleolin, a protein conserved across animals, plants, and fungi, but previously thought to be absent in nematodes. Deleting the RG/RGG repeats within endogenous NUCL-1 and a second nucleolar protein, GARR-1 (GAR1), demonstrates these domains are dispensable for nucleolar accumulation. Instead, their RG/RGG repeats contribute to the phase separation of proteins into nucleolar sub-compartments. Despite this common RG/RGG repeat function, only removal of the GARR-1 RG/RGG domain affects worm fertility and development, decoupling precise sub-nucleolar structure from nucleolar function.

Date: 2022
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DOI: 10.1038/s41467-022-34225-5

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