Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo.

doi:10.1093/nar/gkh751

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Article

Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo.

Nucleic acids research - 1 Jan 2004

Martin Franck, Barends Sharief, Eriani Gilbert

Abstract excerpt

Aminoacyl-tRNA synthetases (aaRSs) are enzymes that are highly specific for their tRNA substrates. Here, we describe the expansion of a class IIb aaRS-tRNA specificity by a genetic selection that involves the use of a modified tRNA displaying an amber anticodon and the argE(amber) and lacZ(amber) reporters. The study was performed on Escherichia coli aspartyl-tRNA synthetase (AspRS) and amber tRNA(Asp). Nine...

Topics

Amino Acid Substitution
Anticodon
Aspartate-tRNA Ligase
Aspartic Acid
Binding Sites
Models, Molecular
Mutation
Phenotype
Protein Engineering
Protein Structure, Tertiary
RNA, Transfer, Amino Acyl

Source

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Identifiers

PMID: 15289581
DOI: 10.1093/nar/gkh751
PMCID: PMC506823

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