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Related Experiment Video

Updated: Jun 10, 2026

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

Codon reassignment in the Escherichia coli genetic code.

Takahito Mukai¹, Akiko Hayashi, Fumie Iraha

¹RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.

Nucleic Acids Research

|August 13, 2010

Summary

Scientists reassigned the UAG genetic code triplet in E. coli by removing a key protein. This demonstrates the genetic code

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Area of Science:

Molecular Biology
Genetics
Microbiology

Background:

The genetic code is largely conserved across life, with 'stop' codons typically terminating protein synthesis.
Reassigning stop codons is thought to be lethal due to mistranslation.

Purpose of the Study:

To investigate the feasibility of reassigning the UAG stop codon to a sense codon in Escherichia coli.
To determine if genetic code flexibility can be achieved without complete genome-wide codon elimination.

Main Methods:

Eliminated the UAG-recognizing release factor (a protein essential for translation termination).
Introduced minimal genetic modifications to E. coli to bypass lethality.
Utilized tRNA specificity to direct UAG decoding to sense amino acids.

Main Results:

Successfully reassigned the UAG triplet from a stop to a sense codon in E. coli.
Demonstrated that complete elimination of UAG triplets from the genome was not required.
Achieved unambiguous assignment of UAG to specific amino acids (natural or non-natural).

Conclusions:

The genetic code exhibits unexpected flexibility.
Codon reassignment is achievable in E. coli with limited genetic manipulation.
This work challenges the notion that the genetic code is irreversibly 'frozen'.