tRNA concentration fine tunes protein solubility
tRNA concentration fine tunes protein solubility
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DOI：
10.1016/j.febslet.2012.07.012
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发表时间：
2012-09-21
期刊：
影响因子：
3.5
通讯作者：
Ignatova, Zoya
中科院分区：
文献类型：
--
作者：
Fedyunin, Ivan;Lehnhardt, Lothar;Ignatova, Zoya
与低丰度tRNA配对的密码子簇使翻译与多结构域蛋白质中单结构域的共翻译折叠同步。尽管有一些例子证明，但核糖体速度对全局、细胞范围水平上的折叠和溶解度的影响仍然难以捉摸。在这里，我们表明，上调三个低丰度的tRNA在大肠杆菌中增加了几种细胞蛋白质的聚集倾向，作为一个结果，加速延伸率。有趣的是，天然tRNA库浓度的改变损害了各种分子伴侣的溶解度，从而使一些分子伴侣依赖性蛋白质溶解。(C)2012年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
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.