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A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A
Abstract Eukaryotic translation elongation factor 1A (eEF1A) is a highly abundant, multi-domain GTPase. Post-translational steps essential for eEF1A biogenesis are carried out by bespoke chaperones but co-translational mechanisms tailored to eEF1A folding remain unexplored.
Zinc-finger protein Zpr1 is a bespoke chaperone essential for eEF1A biogenesis
Balchin D. Hayer-Hartl M. Hartl F.U. In vivo aspects of protein folding and quality control. Science. 2016; 353: aac4354 Molecular chaperones in cellular protein folding. Nature. 1996; 381: 571-579https://doi.org/10.1038/381571a0 The heat-shock proteins. Annu. Rev. Genet. 1988; 22: 631-677https://doi.org/10.1146/annurev.ge.22.120188.003215 Solís E.J. Pandey J.P. Zheng X. Jin D.X. Gupta P.B. Airoldi E.M. Pincus D. Denic V.
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