Refine
Has Fulltext
- no (1)
Year of publication
- 2012 (1) (remove)
Document Type
- Article (1)
Language
- English (1)
Is part of the Bibliography
- yes (1)
Keywords
- E. coli (1) (remove)
Institute
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 Escherichia coil 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.