@article{FedyuninLehnhardtBoehmeretal.2012,
  author    = {Fedyunin, Ivan and Lehnhardt, Lothar and B{\"o}hmer, Nadine and Kaufmann, Paul and Zhang, Gong and Ignatova, Zoya},
  title     = {tRNA concentration fine tunes protein solubility},
  series = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  volume    = {586},
  journal   = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  number    = {19},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0014-5793},
  doi       = {10.1016/j.febslet.2012.07.012},
  pages     = {3336 -- 3340},
  year      = {2012},
  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 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.},
  language  = {en}
}