TY  - JOUR
A1  - Fedyunin, Ivan
A1  - Lehnhardt, Lothar
A1  - Böhmer, Nadine
A1  - Kaufmann, Paul
A1  - Zhang, Gong
A1  - Ignatova, Zoya
T1  - tRNA concentration fine tunes protein solubility
JF  - FEBS letters : the journal for rapid publication of short reports in molecular biosciences
N2  - 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.
KW  - Protein translation
KW  - Protein misfolding
KW  - tRNA
KW  - E. coli
Y1  - 2012
U6  - https://doi.org/10.1016/j.febslet.2012.07.012
SN  - 0014-5793
VL  - 586
IS  - 19
SP  - 3336
EP  - 3340
PB  - Elsevier
CY  - Amsterdam
ER  -