A Rationally Designed Pyrrolysyl-tRNA Synthetase Mutant with a Broad Substrate Spectrum

Together with tRNACUA Pyl, a rationally designed pyrrolysyl-tRNA synthetase mutant N346A/C348A has been successfully used for the genetic incorporation of a variety of phenylalanine derivatives with large para substituents into superfolder green fluorescent protein at an amber mutation site in Esche...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2012-02, Vol.134 (6), p.2950-2953
Main Authors: Wang, Yane-Shih, Fang, Xinqiang, Wallace, Ashley L, Wu, Bo, Liu, Wenshe R
Format: Article
Language:English
Subjects:
Amino Acyl-tRNA Synthetases - genetics
Binding Sites
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Escherichia coli - metabolism
Genetic Engineering - methods
green fluorescent protein
Green Fluorescent Proteins - chemistry
Models, Chemical
mutants
Mutation
nonsense mutation
Nucleic Acid Conformation
Peptides - chemistry
phenylalanine
Phenylalanine - chemistry
Protein Engineering - methods
Pyrroles - chemistry
Substrate Specificity
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Summary:Together with tRNACUA Pyl, a rationally designed pyrrolysyl-tRNA synthetase mutant N346A/C348A has been successfully used for the genetic incorporation of a variety of phenylalanine derivatives with large para substituents into superfolder green fluorescent protein at an amber mutation site in Escherichia coli. This discovery greatly expands the genetically encoded noncanonical amino acid inventory and opens the gate for the genetic incorporation of other phenylalanine derivatives using engineered pyrrolysyl-tRNA synthetase-tRNACUA Pyl pairs.
ISSN:0002-7863
1520-5126
1520-5126
DOI:10.1021/ja211972x