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- Title
tRNA concentration fine tunes protein solubility
- Authors
Fedyunin, Ivan; Lehnhardt, Lothar; Böhmer, Nadine; Kaufmann, Paul; Zhang, Gong; Ignatova, Zoya
- Abstract
Abstract: 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 coli 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.
- Subjects
MOLECULAR chaperones; SOLUBILITY; TRANSFER RNA; CLUSTER analysis (Statistics); GENETIC code; ESCHERICHIA coli
- Publication
FEBS Letters, 2012, Vol 586, Issue 19, p3336
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.07.012