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Activities of 20 aminoacyl-tRNA synthetases expressed in a reconstituted translation system in Escherichia coli.

ABSTRACT: 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.

SUBMITTER: Awai T

PROVIDER: S-EPMC5668874 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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Activities of 20 aminoacyl-tRNA synthetases expressed in a reconstituted translation system in <i>Escherichia coli</i>.

Awai Takako T Ichihashi Norikazu N Yomo Tetsuya T

Biochemistry and biophysics reports 20150808

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 a ...[more]

PMID: 29124177

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