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

Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. It is not clear how this promiscuous mechanism ensure efficient production of challenging clients such as highly expressed proteins. Here we find that the biogenesis of the abundantly expressed eukaryotic translation elongation factor 1A (eEF1A) depends on the dedicated ribosome-associated chaperone Chp1.