Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation

RNA. 2002 Nov;8(11):1363-72. doi: 10.1017/s1355838202021180.


Aminoacyl-tRNA synthetases attach amino acids to the 3' termini of cognate tRNAs to establish the specificity of protein synthesis. A recent Asilomar conference (California, January 13-18, 2002) discussed new research into the structure-function relationship of these crucial enzymes, as well as a multitude of novel functions, including participation in amino acid biosynthesis, cell cycle control, RNA splicing, and export of tRNAs from nucleus to cytoplasm in eukaryotic cells. Together with the discovery of their role in the cellular synthesis of proteins to incorporate selenocysteine and pyrrolysine, these diverse functions of aminoacyl-tRNA synthetases underscore the flexibility and adaptability of these ancient enzymes and stimulate the development of new concepts and methods for expanding the genetic code.

Publication types

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

MeSH terms

  • Amino Acids / metabolism*
  • Amino Acyl-tRNA Synthetases / chemistry
  • Amino Acyl-tRNA Synthetases / physiology*
  • Animals
  • Biological Evolution
  • Eukaryotic Cells / enzymology
  • Genetic Code
  • Humans
  • Protein Biosynthesis
  • Protein Conformation
  • RNA, Transfer / metabolism


  • Amino Acids
  • RNA, Transfer
  • Amino Acyl-tRNA Synthetases