Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding

Daniel A. Nissley, Ajeet K. Sharma, Nabeel Ahmed, Ulrike A. Friedrich, Günter Kramer, Bernd Bukau and Edward P. O’Brien ()
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Daniel A. Nissley: Pennsylvania State University
Ajeet K. Sharma: Pennsylvania State University
Nabeel Ahmed: Bioinformatics and Genomics Graduate Program, The Huck Institutes of the Life Sciences, Pennsylvania State University
Ulrike A. Friedrich: Center for Molecular Biology of the University of Heidelberg (ZMBH)
Günter Kramer: Center for Molecular Biology of the University of Heidelberg (ZMBH)
Bernd Bukau: Center for Molecular Biology of the University of Heidelberg (ZMBH)
Edward P. O’Brien: Pennsylvania State University

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract The rates at which domains fold and codons are translated are important factors in determining whether a nascent protein will co-translationally fold and function or misfold and malfunction. Here we develop a chemical kinetic model that calculates a protein domain’s co-translational folding curve during synthesis using only the domain’s bulk folding and unfolding rates and codon translation rates. We show that this model accurately predicts the course of co-translational folding measured in vivo for four different protein molecules. We then make predictions for a number of different proteins in yeast and find that synonymous codon substitutions, which change translation-elongation rates, can switch some protein domains from folding post-translationally to folding co-translationally—a result consistent with previous experimental studies. Our approach explains essential features of co-translational folding curves and predicts how varying the translation rate at different codon positions along a transcript’s coding sequence affects this self-assembly process.

Date: 2016
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DOI: 10.1038/ncomms10341

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