RG/RGG repeats in the C. elegans homologs of Nucleolin and GAR1 contribute to sub-nucleolar phase separation
Abstrak
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. Spaulding et al. survey RG/RGG repeats in C. elegans and identify the homologs of Nucleolin (NUCL-1) and GAR1 (GARR-1). RG/RGG repeats are dispensable for nucleolar accumulation but critical for sub-nucleolar phase separation.
Topik & Kata Kunci
Penulis (4)
E. Spaulding
Alexis M. Feidler
Lio A. Cook
Dustin L. Updike
Akses Cepat
- Tahun Terbit
- 2022
- Bahasa
- en
- Total Sitasi
- 32×
- Sumber Database
- Semantic Scholar
- DOI
- 10.1038/s41467-022-34225-5
- Akses
- Open Access ✓