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 |