Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers.
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.
Park
Sang Gyu
SG
National Creative Research Initiatives Center for ARS Network, College of Pharmacy, Seoul National University, San 56-1, Shillim-dong, Kwanak-gu, Seoul 151-742, Korea.
Ewalt
Karla L
KL
Kim
Sunghoon
S
D000596:Amino Acids / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D017209:Apoptosis / Q000502:physiology; D004260:DNA Repair; D019204:GTP-Binding Proteins / Q000502:physiology*; D006801:Humans; D007249:Inflammation; D046911:Macromolecular Substances; D018919:Neovascularization, Physiologic / Q000502:physiology; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000378:metabolism
D000596:Amino Acids; D046911:Macromolecular Substances; D012343:RNA, Transfer; D019204:GTP-Binding Proteins; D000604:Amino Acyl-tRNA Synthetases