A simple structural feature is a major determinant of the identity of a transfer RNA.
Analysis of a series of mutants of an Escherichia coli alanine transfer RNA shows that substitution of a single G-U base pair in the acceptor helix eliminates aminoacylation with alanine in vivo and in vitro. Introduction of that base pair into the analogous position of a cysteine and a phenylalanine transfer RNA confers upon each the ability to be aminoacylated with alanine. Thus, as little as a single base pair can direct an amino acid to a specific transfer RNA.
Hou
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Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Schimmel
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D001482:Base Composition; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D009690:Nucleic Acid Conformation; D012344:RNA, Transfer, Ala / Q000235:genetics*; D012345:RNA, Transfer, Amino Acid-Specific / Q000235:genetics*; D013489:Suppression, Genetic
D012344:RNA, Transfer, Ala; D012345:RNA, Transfer, Amino Acid-Specific