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Transforming a pair of orthogonal trna-aminoacyl-trna synthetase from archaea to function in mammalian (2010).
| Content Provider | CiteSeerX |
|---|---|
| Author | Thibodeaux, Gabrielle Nina Liang, Xiang Moncivais, Kathryn Umeda, Aiko Singer, Oded Zhang, Zhiwen Jonathan |
| Abstract | A previously engineered Methanocaldococcus jannaschii tRNA Tyr CUA –tyrosyl-tRNA synthetase pair orthogonal to Escherichia coli was modified to become orthogonal in mammalian cells. The resulting tRNA Tyr CUA-tyrosyl-tRNA synthetase pair was able to suppress an amber codon in the green fluorescent protein, GFP, and in a foldon protein in mammalian cells. The methodology reported here will allow rapid transformation of the much larger collection of existing tyrosyl-tRNA synthetases that were already evolved for the incorporation of an array of over 50 unnatural amino acids into proteins in Escherichia coli into proteins in mammalian cells. Thus we will be able to introduce a large array of possibilities for protein |
| File Format | |
| Publisher Date | 2010-01-01 |
| Access Restriction | Open |
| Subject Keyword | Mammalian Cell Orthogonal Trna-aminoacyl-trna Synthetase Foldon Protein Rapid Transformation Tyrosyl-trna Synthetases Green Fluorescent Protein Amber Codon Large Array Escherichia Coli Trna Tyr Cua-tyrosyl-trna Synthetase Pair Unnatural Amino Acid |
| Content Type | Text |
