RG/RGG repeats in the C. elegans homologs of Nucleolin and GAR1 contribute to sub-nucleolar phase separation
Year: 2022
Type: article
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.
Source: Nature Communications
Institution: Mount Desert Island Biological Laboratory
Language: English
Topic: RNA Research and Splicing
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,890
Awards: REU Site: Comparative Approaches in Cellular, Molecular and Environmental Biology, Comparative Biology of Tissue Repair, Regeneration and Aging, G283890573, G4458519119, G4790291344, The function of germ granules in maintaining pluripotency in the C. elegans germline, G5835006330, G6639879970, Understanding how Vasa Proteins Promote Cellular Pluripotency in the C. elegans Germline, G8571787556, The Maine Biomedical Research Network (INBRE)
OpenAlex ID: W4308486097