22TU

Human 80S ribosome in complex with DHX29

This is a non-PDB format compatible entry.

Summary for 22TU

• Entry DOI: 10.2210/pdb22tu/pdb
• EMDB information: 68666
• Descriptor: 60S ribosomal protein L8, 60S ribosomal protein L5, 60S ribosomal protein L6, ... (84 entities in total)
• Functional Keywords: ribosome, translation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 83
• Total formula weight: 4000582.15

Authors

Goto-Ito, S.,Iwasaki, W.,Ito, T. (deposition date: 2026-01-22, release date: 2026-04-01)

Primary citation

Hia, F.,Wu, Y.,Yoshinaga, M.,Goto-Ito, S.,Iwasaki, W.,Imami, K.,Toh, H.,Han, P.,Cai, T.,Ohira, T.,Fukao, A.,Standley, D.M.,Shichino, Y.,Takegawa, M.,Fujiwara, T.,Suzuki, T.,Iwasaki, S.,Bassik, M.C.,Ito, T.,Takeuchi, O.
Human DHX29 detects nonoptimal codon usage to regulate mRNA stability.
Science, :eadw0288-eadw0288, 2026

PubMed Abstract: Synonymous codon usage controls global gene expression in both prokaryotic and eukaryotic species. Nonoptimal codons are known to induce mRNA decay; however, the underlying molecular mechanism remains poorly understood in human cells. Through genome-wide CRISPR screening, we identified the RNA-binding protein DHX29 as a critical regulator of codon-dependent gene expression. Cryogenic electron microscopy and selective ribosome profiling demonstrated that DHX29 directly interacts with the A-site entrance of the translating 80S ribosome, the binding site for the eEF1A•GTP•aminoacyl-tRNA ternary complex, suggesting a role in monitoring aminoacyl-tRNA sampling. Proteomic analysis further revealed that DHX29 recruits the GIGYF2•4EHP complex to mediate global suppression of nonoptimal mRNAs. These findings establish a mechanistic link between synonymous codon usage and the regulation of gene expression.

PubMed: 41855277
DOI: 10.1126/science.adw0288

Experimental method

ELECTRON MICROSCOPY (3 Å)