5W4D

C. japonica N-domain, Selenomethionine mutant

Summary for 5W4D

• Entry DOI: 10.2210/pdb5w4d/pdb
• Descriptor: P-granule scaffold protein, 1,2-ETHANEDIOL, TRIETHYLENE GLYCOL, ... (9 entities in total)
• Functional Keywords: p-granule scaffold protein, rna binding protein
• Biological source: Caenorhabditis japonica
• Total number of polymer chains: 4
• Total formula weight: 100309.06

Authors

Aoki, S.T.,Bingman, C.A.,Kimble, J. (deposition date: 2017-06-10, release date: 2018-06-13, Last modification date: 2024-10-16)

Primary citation

Aoki, S.T.,Lynch, T.R.,Crittenden, S.L.,Bingman, C.A.,Wickens, M.,Kimble, J.
C. elegans germ granules require both assembly and localized regulators for mRNA repression.
Nat Commun, 12:996-996, 2021

PubMed Abstract: 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 Å, 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.

PubMed: 33579952
DOI: 10.1038/s41467-021-21278-1

Experimental method

X-RAY DIFFRACTION (1.599 Å)