tRNA concentration fine tunes protein solubility

被引：61

作者：

Fedyunin, Ivan ^{[1
,2
]}

Lehnhardt, Lothar ^{[1
]}

Boehmer, Nadine ^{[1
]}

Kaufmann, Paul ^{[1
]}

Zhang, Gong ^{[1
]}

Ignatova, Zoya ^{[1
]}

机构：

[1] Univ Potsdam, Inst Biochem & Biol, D-14476 Potsdam, Germany

[2] Max Planck Inst Colloids & Interfaces, IMPRS Grad Sch, D-14424 Potsdam, Germany

来源：

FEBS LETTERS | 2012年 / 586卷 / 19期

关键词：

Protein translation; Protein misfolding; tRNA; E; coli; ESCHERICHIA-COLI; CODON USAGE; TRANSLATIONAL ELONGATION; NASCENT POLYPEPTIDE; TRIGGER FACTOR; RIBOSOME; GENOME; BIAS; DETERMINANTS; ATTENUATION;

D O I：

10.1016/j.febslet.2012.07.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：3336 / 3340

页数：5

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