PMID:1959653
| Citation |
Kast, P, Wehrli, C and Hennecke, H (1991) Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases. FEBS Lett. 293:160-3 |
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| Abstract |
Phenylalanyl-tRNA synthetase (PheRS; alpha 2 beta 2 subunit structure) is a member of class II of tRNA synthetases. We report here the genetic analysis of an Escherichia coli mutant strain which is auxotrophic for phenylalanine because it has a PheRS with a decreased affinity for phenylalanine. The mutant pheS gene encoding the PheRS alpha subunit was cloned and sequenced, and the deviation from the wild-type gene was found to result in a Gly191-to-Asp191 exchange. This alteration is located within motif 2, one of 3 conserved sequence motifs characteristic for class II aminoacyl-tRNA synthetases. Motif 2 may thus participate in the formation of the phenylalanine binding site in PheRS. |
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| Keywords |
Amino Acid Sequence; Amino Acids/genetics; Aspartic Acid/genetics; Cloning, Molecular; Consensus Sequence; Escherichia coli/enzymology; Escherichia coli/genetics; Genetic Vectors; Glycine/genetics; Molecular Sequence Data; Mutation; Phenylalanine/genetics; Phenylalanine-tRNA Ligase/classification; Phenylalanine-tRNA Ligase/genetics |
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