tRNA concentration fine tunes protein solubility
- 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.
| Author details: | Ivan Fedyunin, Lothar Lehnhardt, Nadine Böhmer, Paul Kaufmann, Gong Zhang, Zoya Ignatova |
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| DOI: | https://doi.org/10.1016/j.febslet.2012.07.012 |
| ISSN: | 0014-5793 |
| Title of parent work (English): | FEBS letters : the journal for rapid publication of short reports in molecular biosciences |
| Publisher: | Elsevier |
| Place of publishing: | Amsterdam |
| Publication type: | Article |
| Language: | English |
| Year of first publication: | 2012 |
| Publication year: | 2012 |
| Release date: | 2017/03/26 |
| Tag: | E. coli; Protein misfolding; Protein translation; tRNA |
| Volume: | 586 |
| Issue: | 19 |
| Number of pages: | 5 |
| First page: | 3336 |
| Last Page: | 3340 |
| Funding institution: | EU Grant (ITN NICHE) |
| Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
| Peer review: | Referiert |
