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Updated: Mar 21, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

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Published on: December 9, 2017

Genetic Code Expansion by Degeneracy Reprogramming of Arginyl Codons.

Ki Baek Lee¹, Chen Yuan Hou¹, Chae-Eun Kim¹

¹Department of Chemical and Biochemical Engineering, Dongguk University-Seoul, Seoul, 100-715, South Korea.

Chembiochem : a European Journal of Chemical Biology

|May 7, 2016

Summary

Researchers created reprogrammable codons to expand the genetic code beyond 20 amino acids. This novel method uses a cell-free system to incorporate non-proteinogenic amino acids, enhancing protein synthesis capabilities.

Keywords:

colicin D degenerate codons mutagenesis protein engineering tRNA

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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

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Published on: December 26, 2020

Area of Science:

Synthetic Biology
Molecular Biology
Biochemistry

Background:

The standard genetic code typically encodes 20 proteinogenic amino acids and translation stop signals.
Expanding the amino acid repertoire often involves reprogramming stop codons, which usually permits the incorporation of only one non-proteinogenic amino acid.

Purpose of the Study:

To develop a novel method for incorporating non-proteinogenic amino acids into proteins using sense codons.
To create reprogrammable codons within a cell-free protein synthesis system.

Main Methods:

Utilized a cell-free protein synthesis system.
Employed colicin D, a tRNA(Arg)-specific ribonuclease, to eliminate endogenous tRNA(Arg).
Supplemented the system with a modified tRNA (tRNACCU) to partially restore translation.

Main Results:

Successfully created reprogrammable codons by selectively degrading tRNA(Arg).
Demonstrated the incorporation of modified lysines alongside the standard 20 proteinogenic amino acids.
Established a system capable of encoding more than 20 amino acids.

Conclusions:

This innovative approach enables the creation of novel codons for expanded genetic encoding.
The method offers a versatile platform for introducing non-proteinogenic amino acids into proteins, advancing synthetic biology and protein engineering.