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Trends Biochem Sci. 2005 Oct;30(10):569-74.

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

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  • 1National Creative Research Initiatives Center for ARS Network, College of Pharmacy, Seoul National University, San 56-1, Shillim-dong, Kwanak-gu, Seoul 151-742, Korea.

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.

PMID:
16125937
[PubMed - indexed for MEDLINE]
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