Abstract
Transfer RNA (tRNA) identify is maintained by the highly specific interaction of a few defined nucleotides or groups of nucleotides, called identity elements, with the cognate aminoacyl-tRNA synthetase, and by nonproductive interactions with the other 19 aminoacyl-tRNA synthetases. Most tRNAs have a set of identity elements in at least two locations, commonly in the anticodon loop or in the acceptor stem, and at the discriminator base position 73. We have used T7 RNA polymerase transcribed tRNAs to demonstrate that the sole replacement of the discriminator base A73 of human tRNA(Leu) with the tRNA(Ser)-specific G generates a complete identity switch to serine acceptance. The reverse experiment, the exchange of G73 in human tRNA(Ser) for the tRNA(Leu-specific A, causes a total loss of serine specificity without creating any leucine acceptance. These results suggest that the discriminator base A73 of human tRNA(Leu) alone protects this tRNA against serylation by seryl-tRNA synthetase. This is the first report of a complete identity switch caused by an exchange of the discriminator base alone.
MeSH Terms
Acylation
Adenine/metabolism
Base Sequence
DNA-Directed RNA Polymerases
Guanine/metabolism
Humans
Leucine/metabolism
Molecular Sequence Data
Mutagenesis
Nucleic Acid Conformation
Protein Biosynthesis
RNA, Transfer, Leu/chemistry,genetics,metabolism
RNA, Transfer, Ser/chemistry,metabolism
Serine/metabolism
Viral Proteins
Chemicals
RNA, Transfer, Leu
RNA, Transfer, Ser
Viral Proteins
Serine
Guanine
bacteriophage T7 RNA polymerase
DNA-Directed RNA Polymerases
Leucine
Adenine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Breitschopf K
Institut für Biochemie, Bayerische Julius-Maximilians-Universität, Würzburg, Germany.
Gross H J
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