One polypeptide with two aminoacyl-tRNA synthetase activities Academic Article Article uri icon


MeSH Major

  • Gastrointestinal Microbiome
  • Infection
  • Inflammation
  • Neoplasms


  • The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro). The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.

publication date

  • January 21, 2000



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1126/science.287.5452.479

PubMed ID

  • 10642548

Additional Document Info

start page

  • 479

end page

  • 82


  • 287


  • 5452