Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations.

ABSTRACT: In all genomes, most amino acids are encoded by more than one codon. Synonymous codons can modulate protein production and folding, but the mechanism connecting codon usage to protein homeostasis is not known. Here we show that synonymous codon variants in the gene encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotranslational folding of protein domains monitored in real time by Förster resonance energy transfer and fluorescence-intensity changes. Gamma-B crystallins produced from mRNAs with changed codon bias have the same amino acid sequence but attain different conformations, as indicated by altered in vivo stability and in vitro protease resistance. 2D NMR spectroscopic data suggest that structural differences are associated with differ

SUBMITTER: Buhr F 

PROVIDER: S-EPMC4745992 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature