Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: New perspectives on housekeepers

Gyu Park Sang, Karla L. Ewalt, Sunghoon Kim

Research output: Contribution to journalReview article

191 Citations (Scopus)

Abstract

Aminoacyl-tRNA synthetases (ARSs) are essential enzymes that join amino acids to tRNAs, thereby linking the genetic code to specific amino acids. Once considered a class of 'housekeeping' enzymes, ARSs are now known to participate in a wide variety of functions, including transcription, translation, splicing, inflammation, angiogenesis and apoptosis. Three nonenzymatic proteins - ARS-interacting multi-functional proteins (AIMPs) - associate with ARSs in a multi-synthetase complex of higher eukaryotes. Similarly to ARSs, AIMPs have novel functions unrelated to their support role in protein synthesis, acting as a cytokine to control angiogenesis, immune response and wound repair, and as a crucial regulator for cell proliferation and DNA repair. Evaluation of the functional roles of individual ARSs and AIMPs might help to elucidate why these proteins as a whole contribute such varied functions and interactions in complex systems.

Original languageEnglish
Pages (from-to)569-574
Number of pages6
JournalTrends in Biochemical Sciences
Volume30
Issue number10
DOIs
Publication statusPublished - 2005 Oct 1

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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