Beschreibung:
<jats:p>Clusters of codons pairing to low‐abundance tRNAs synchronize the translation with co‐translational folding of single domains in multidomain proteins. Although proven with some examples, the impact of the ribosomal speed on the folding and solubility on a global, cell‐wide level remains elusive. Here we show that upregulation of three low‐abundance tRNAs in <jats:italic>Escherichia coli</jats:italic> increased the aggregation propensity of several cellular proteins as a result of an accelerated elongation rate. Intriguingly, alterations in the concentration of the natural tRNA pool compromised the solubility of various chaperones consequently rendering the solubility of some chaperone‐dependent proteins.</jats:p>