Aminoacyl-tRNA synthetases: A new image for a classical family

Susan A. Martinis, Pierre Plateau, Jean Cavarelli, Catherine Florentz

Research output: Contribution to journalReview articlepeer-review

Abstract

The aminoacyl-tRNA synthetases (aaRSs) are a family of enzymes well known for their role in protein synthesis. More recent investigations have discovered that this classic family of enzymes is actually capable of a broad repertoire of functions which not only impact protein synthesis, but extend to a number of other critical cellular activities. Specific aaRSs play roles in cellular fidelity, tRNA processing, RNA splicing, RNA trafficking, apoptosis, transcriptional and translational regulation. A recent EMBO workshop entitled 'Structure and Function of Aminoacyl-tRNA Synthetases' (Mittelwihr, France, October 10-15, 1998), highlighted the diversity of the aaRSs' role within the cell. These novel activities as well as significant advances in delineating mechanisms of substrate specificity and the aminoacylation reaction affirm the family of aaRSs as pharmaceutical targets.

Original languageEnglish (US)
Pages (from-to)683-700
Number of pages18
JournalBiochimie
Volume81
Issue number7
DOIs
StatePublished - Jul 1999
Externally publishedYes

Keywords

  • Aminoacyl-tRNA synthetases
  • Antibiotic
  • Molecular evolution
  • Protein synthesis
  • RNA recognition
  • tRNA identity

ASJC Scopus subject areas

  • Biochemistry

Fingerprint

Dive into the research topics of 'Aminoacyl-tRNA synthetases: A new image for a classical family'. Together they form a unique fingerprint.

Cite this