High impact information on Rars

• Arginyl-tRNA synthetase, elongation factor 1a, ribosomal RNA, and myelin basic protein mRNA were all co-localized in granules in the processes, veins and membrane sheets of the cell [1].
• L-canavanine can be charged by arginyl tRNA synthetase to replace L-arginine during protein synthesis [2].
• Proteins of M(r) 140, 60, 57, 50, 22, and 14 kDa, all possessing arginyl-tRNA synthetase activity, were subjected to phosphorylation without addition of exogenous protein kinase activity [3].
• Two, F7 and F31 were directed against arginyl-tRNA synthetase, two, F8 and F25 against glutamyl-tRNA synthetase, and two, F6 and F12 recognised 38 and 43 kDa polypeptides, respectively [4].

Biological context of Rars

• Phosphorylation/dephosphorylation experiments with arginyl-tRNA synthetase indicate that the peaks represent phosphorylated and unphosphorylated synthetase protein [5].

Analytical, diagnostic and therapeutic context of Rars

• Purification was performed by either gel filtration on Sephadex G-200 or chromatofocusing before affinity chromatography on immobilized total tRNA (mixture of tRNA's, specific for all aminoacyl-tRNA synthetases), followed by affinity chromatography on immobilized tRNA, specific for arginyl-tRNA synthetase [6].

References