Activities of 20 aminoacyl-tRNA synthetases expressed in a reconstituted translation system in Escherichia coli.
Activities of 20 aminoacyl-tRNA synthetases expressed in a reconstituted translation system in Escherichia coli.
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DOI：
10.1016/j.bbrep.2015.08.006
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发表时间：
2015-09
影响因子：
2.7
通讯作者：
Yomo T
中科院分区：
文献类型：
--
作者：
Awai T;Ichihashi N;Yomo T
A significant challenge in the field of in vitro synthetic biology is the construction of a self-reproducing cell-free translation system, which reproduces its components, such as translation proteins, through translation and transcription by itself. As a first step for such construction, in this study we expressed and evaluated the activity of 20 aminoacyl-tRNA synthetases (aaRSs), a major component of a translation system, in a reconstituted translation system (PURE system). We found that 19 aaRS with the exception of phenylalanyl-tRNA synthetase (PheRS) are expressed as soluble proteins and their activities are comparable to those expressed in Escherichia coli . This study provides basic information on the properties of aaRSs expressed in the PURE system, which will be helpful for the future reconstitution of a self-reproducing translation system. We expressed 20 aminoacyl-tRNA synthetases in a reconstituted translation system. All aminoacyl-tRNA synthetases (aaRSs) are expressed as soluble proteins. All aaRSs with the exception of phenylalanyl-tRNA synthetase are active. Their activities are comparable to those expressed in E. coli.
