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Exploring the Substrate Range of Wild‐Type Aminoacyl‐tRNA Synthetases
Author(s) -
Fan Chenguang,
Ho Joanne M. L.,
Chirathivat Napon,
Söll Dieter,
Wang YaneShih
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402083
Subject(s) - aminoacyl trna synthetase , transfer rna , amino acid , amino acyl trna synthetases , substrate (aquarium) , biochemistry , biology , peptide sequence , translation (biology) , substrate specificity , enzyme , rna , messenger rna , gene , ecology
We tested the substrate range of four wild‐type E. coli aminoacyl‐tRNA synthetases (AARSs) with a library of nonstandard amino acids (nsAAs). Although these AARSs could discriminate efficiently against the other canonical amino acids, they were able to use many nsAAs as substrates. Our results also show that E. coli tryptophanyl‐tRNA synthetase (TrpRS) and tyrosyl‐tRNA synthetase have overlapping substrate ranges. In addition, we found that the nature of the anticodon sequence of tRNA Trp altered the nsAA substrate range of TrpRS; this implies that the sequence of the anticodon affects the TrpRS amino acid binding pocket. These results highlight again that inherent AARS polyspecificity will be a major challenge in the aim of incorporating multiple different amino acids site‐specifically into proteins.