The role of anticodon bases and the discriminator nucleotide in the recognition of some E. coli tRNAs by their aminoacyl-tRNA synthetases

J Mol Evol. 1992 Nov;35(5):436-43. doi: 10.1007/BF00171822.

Abstract

The T7 polymerase transcription system was used for in vitro synthesis of unmodified versions of the E. coli tRNA mutants that insert asparagine, cysteine, glycine, histidine, and serine. These tRNAs were used to qualitatively explore the role of some anticodon bases and the discriminator nucleotide in the recognition of tRNA by aminoacyl-tRNA synthetases. Coupled with data from earlier studies, these new results essentially complete a survey of all E. coli tRNAs with respect to the involvement of anticodon bases and the discriminator nucleotide in tRNA recognition. It is found that in the vast majority of tRNAs both of these elements are significant components of tRNA identity. This is not universally true, however. Anticodon sequences are unimportant in tRNA(Ser), tRNA(Leu), and tRNA(Ala) while the discriminator base is inconsequential in tRNA(Ser) and tRNA(Thr). The significance of these results for origin-of-life studies is discussed.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acyl-tRNA Synthetases / metabolism*
  • Anticodon / genetics*
  • Asparagine / metabolism
  • Bacteriophage T7
  • Base Sequence
  • Cysteine / metabolism
  • DNA-Directed RNA Polymerases
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Glycine / metabolism
  • Histidine / metabolism
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • RNA, Transfer / genetics*
  • RNA, Transfer / metabolism
  • Serine / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Anticodon
  • Serine
  • Histidine
  • Asparagine
  • RNA, Transfer
  • DNA-Directed RNA Polymerases
  • Amino Acyl-tRNA Synthetases
  • Cysteine
  • Glycine