tRNAPhe deprived of 3'-terminal adenosyl residue does not stimulate adenosine aminoacylation catalyzed by phenylalanyl-tRNA synthetase from Escherichia coli

FEBS Lett. 1988 Sep 26;238(1):211-3. doi: 10.1016/0014-5793(88)80258-8.

Abstract

Phenylalanyl-tRNA synthetase from Escherichia coli does not catalyze the [14C]phenylalanyl residue transfer from phenylalanyl-adenylate to adenosine either in the presence or absence of homologous tRNAPhe and tRNA(-A Phe). When the reaction mixture contained dithiothreitol, radioactive substance was detected having a mobility on HPLC column close to that of aminoacyladenosine. The amount of this product depended on the concentration of dithiothreitol in the mixture. Phenylalanyl residue was suggested to undergo transfer from aminoacyladenylate to dithiothreitol molecule.

MeSH terms

  • Acylation
  • Adenosine*
  • Amino Acyl-tRNA Synthetases / metabolism*
  • Carbon Radioisotopes
  • Dithiothreitol / pharmacology
  • Escherichia coli / enzymology*
  • Phenylalanine-tRNA Ligase / metabolism*
  • RNA, Transfer, Amino Acid-Specific / metabolism*
  • RNA, Transfer, Phe / metabolism*
  • Substrate Specificity

Substances

  • Carbon Radioisotopes
  • RNA, Transfer, Amino Acid-Specific
  • RNA, Transfer, Phe
  • Amino Acyl-tRNA Synthetases
  • Phenylalanine-tRNA Ligase
  • Adenosine
  • Dithiothreitol