5W4D

C. japonica N-domain, Selenomethionine mutant

5W4D の概要

• エントリーDOI: 10.2210/pdb5w4d/pdb
• 分子名称: P-granule scaffold protein, 1,2-ETHANEDIOL, TRIETHYLENE GLYCOL, ... (9 entities in total)
• 機能のキーワード: p-granule scaffold protein, rna binding protein
• 由来する生物種: Caenorhabditis japonica
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 100309.06

構造登録者

Aoki, S.T.,Bingman, C.A.,Kimble, J. (登録日: 2017-06-10, 公開日: 2018-06-13, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.599 Å)