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Related Experiment Video

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Super-Resolution Imaging of Bacterial Secreted Proteins Using Genetic Code Expansion

Super-Resolution Imaging of Bacterial Secreted Proteins Using Genetic Code Expansion

Published on: February 10, 2023

An orthogonalized platform for genetic code expansion in both bacteria and eukaryotes.

James S Italia¹, Partha Sarathi Addy¹, Chester J J Wrobel¹

¹Department of Chemistry, Boston College, Chestnut Hill, Massachusetts, USA.

Nature Chemical Biology

|February 14, 2017

Summary

Scientists expanded the genetic code of E. coli using its own tryptophanyl-tRNA synthetase and tRNA (TrpRS-tRNA^Trp) pair. This method enables the creation of new unnatural amino acids (UAAs) in both bacteria and mammalian cells.

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Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays

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Published on: November 12, 2012

Area of Science:

Synthetic Biology
Molecular Biology
Genetics

Background:

The genetic code's expansion allows for the incorporation of unnatural amino acids (UAAs) into proteins, enabling novel functionalities.
Developing versatile systems for UAA incorporation in both prokaryotic and eukaryotic systems remains a challenge.

Purpose of the Study:

To demonstrate the feasibility of expanding the genetic code of Escherichia coli using its endogenous tryptophanyl-tRNA synthetase and tRNA (TrpRS-tRNA^Trp) pair.
To engineer this system for directed evolution to create new UAAs.
To assess the utility of the engineered system for UAA mutagenesis in mammalian cells.

Main Methods:

Functional replacement of the endogenous E. coli TrpRS-tRNA^Trp pair with a Saccharomyces cerevisiae-optimized counterpart.
Reintroduction of the liberated E. coli TrpRS-tRNA^Trp pair as a nonsense suppressor.
Directed evolution of the TrpRS-tRNA^Trp pair to genetically encode new UAAs.
Testing the engineered variants for UAA mutagenesis in mammalian cells.

Main Results:

Successfully demonstrated the feasibility of expanding the genetic code in E. coli using its native TrpRS-tRNA^Trp pair.
Engineered TrpRS-tRNA^Trp variants capable of genetically encoding several new UAAs.
Achieved efficient UAA mutagenesis in mammalian cells using the engineered bacterial-derived TrpRS-tRNA^Trp variants.

Conclusions:

The study presents a viable strategy for expanding the genetic code of E. coli.
The developed system allows for the creation of novel UAAs through directed evolution.
This approach provides a generalizable method for developing aminoacyl-tRNA synthetase-tRNA pairs for UAA mutagenesis in both bacteria and eukaryotes.