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Yielding at stop codons: expanding the genetic code.

Tamara L Hendrickson¹

¹Johns Hopkins University, Department of Chemistry, 3400 N. Charles Street, Baltimore, MD 21218, USA.

Chemistry & Biology

|July 3, 2003

Summary

Researchers can now genetically encode non-native amino acids into proteins using a novel selection method. This technique successfully identified specific enzymes in E. coli and yeast for protein diversification.

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Putting amino acids onto tRNAs: The aminoacyl-tRNA synthetases as catalysts.

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Area of Science:

Biochemistry
Molecular Biology
Synthetic Biology

Background:

The genetic code allows for the creation of diverse proteins.
Incorporating non-native amino acids expands protein functionality.

Purpose of the Study:

To develop a method for isolating enzymes that can attach non-native amino acids to transfer RNAs (tRNAs).
To demonstrate the utility of this method in both bacterial (E. coli) and yeast (S. cerevisiae) systems.

Main Methods:

Utilizing iterative rounds of selection to identify desired aminoacyl-tRNA synthetases.
Employing suppressor tRNAs to accept non-native amino acids.

Main Results:

Successfully isolated specific aminoacyl-tRNA synthetases capable of aminoacylating suppressor tRNAs with non-native amino acids.
Demonstrated the effectiveness of the selection process in both E. coli and S. cerevisiae.

Conclusions:

Iterative selection is an effective strategy for engineering aminoacyl-tRNA synthetases for non-native amino acid incorporation.
This method provides a powerful tool for expanding the proteome and diversifying protein function.

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