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tRNA specificity of a mischarging aminoacyl‐tRNA synthetase: Glutamyl‐tRNA synthetase from barley chloroplasts
Author(s) -
Schön Astrid,
Söll Dieter
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80007-3
Subject(s) - transfer rna , chloroplast , biochemistry , heterologous , aminoacyl trna synthetase , enzyme , biology , chemistry , rna , gene
Glutamyl‐tRNA synthetase (GluRS) from barley chloroplasts is a naturally occurring mischarging enzyme: it efficiently aminoacylates both the homologous tRNA Glu as well as tRNA Gln species. In order to shed light on the structural requirements of this enzyme for tRNA specificity heterologous charging experiments were performed. Sequence comparison of tRNAs recognized by barley chloroplast GluRS reveals that two base pairs, one in the acceptor stem and one in the anticodon stem, appear to be critical for substrate recognition.