期刊
FEBS LETTERS
卷 586, 期 19, 页码 3336-3340出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.07.012
关键词
Protein translation; Protein misfolding; tRNA; E. coli
资金
- EU Grant (ITN NICHE)
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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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