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Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis

15 Feb 2024

Abstract excerpt

Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated chaperone, Chp1, that rewires the cotranslational folding machinery to assist in the challenging biogenesis of abundantly expressed eukaryotic translation elongation factor 1A (eEF1A). Our results indicate that during eEF1A synthesis, Chp1 is...

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PMID: 38360885
DOI: 10.1038/s41467-024-45645-w

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