A provisional mechanism for regulating the aminoacyl-tRNA synthetases.
A mechanism is outlined for regulating aminoacyl-tRNA synthetases with a nonheme iron-containing protein serving as the key regulator. This mechanism is formulated from experiments with a complex-bound valyl-tRNA synthetase from yeast that is activated by thiols, by tRNA, and by an iron-containing protein preparation with characteristic spectral properties.
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Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation; D005656:Fungal Proteins / Q000378:metabolism; D005978:Glutathione / Q000494:pharmacology; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D015636:Magnesium Chloride / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D008667:Metalloproteins / Q000378:metabolism*; D012343:RNA, Transfer / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013053:Spectrophotometry; D014637:Valine-tRNA Ligase / Q000378:metabolism*
D005656:Fungal Proteins; D008667:Metalloproteins; D015636:Magnesium Chloride; D008623:Mercaptoethanol; D012343:RNA, Transfer; D007501:Iron; D000604:Amino Acyl-tRNA Synthetases; D014637:Valine-tRNA Ligase; D005978:Glutathione; D004229:Dithiothreitol