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Related Experiment Video

Updated: Jun 13, 2025

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

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

Published on: December 9, 2017

Efficient genetic code expansion without host genome modifications.

Alan Costello^1,2, Alexander A Peterson^1,2, David L Lanster^1,2,3

¹Department of Chemistry, The Scripps Research Institute, La Jolla, CA, USA.

Nature Biotechnology

|September 11, 2024

Summary

This summary is machine-generated.

This study introduces a novel codon compression strategy for efficient noncanonical amino acid (ncAA) incorporation in proteins. This method enhances genetic code expansion and enables the creation of diverse new-to-nature biomolecules.

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Area of Science:

Synthetic Biology
Molecular Biology
Biochemistry

Background:

Existing methods for incorporating noncanonical amino acids (ncAAs) into proteins often face challenges with low efficiency and context dependency.
Genetic code expansion aims to create proteins with novel functions by incorporating unnatural amino acids.

Purpose of the Study:

To develop a more efficient and context-independent strategy for ncAA incorporation using codon compression.
To identify and optimize transfer RNA (tRNA)-synthetase pairs for expanded genetic codes.
To establish an in vivo biosynthesis platform for creating novel peptide macrocycles.

Main Methods:

A plasmid-based codon compression strategy was developed using conventional Escherichia coli strains and native ribosomes.
The strategy focused on utilizing quadruplet codons for improved ncAA incorporation efficiency.
Multiple mutually orthogonal tRNA-synthetase pairs were identified and optimized for incorporating a wide range of ncAAs.

Main Results:

The developed codon compression strategy significantly improved ncAA incorporation efficiency at quadruplet codons while minimizing context dependence.
Twelve mutually orthogonal tRNA-synthetase pairs were identified, and five were further evolved for broader ncAA incorporation.
An in vivo biosynthesis platform was established, enabling the creation of over 100 new-to-nature peptide macrocycles with up to three unique ncAAs.

Conclusions:

Codon usage is a critical, previously unrecognized factor in efficient genetic code expansion.
The developed strategy and resources accelerate innovations in multiplexed genetic code expansion.
This work facilitates the discovery and production of chemically diverse biomolecules with novel functions.