Glutamyl-tRNA synthetases from wheat. Isolation and characterization of three dimeric enzymes.
Three dimeric glutamyl-tRNA synthetases (GluRS) were isolated from extracts of quiescent wheat germ and wheat chloroplasts. The chloroplast enzyme (Mr = 110 000), called GluRS C, exhibits a prokaryotic (Escherichia coli) tRNA specificity. Two enzymes were found in the quiescent germ and were separated on phosphocellulose P11: one called GluRS P, probably the mitochondrial enzyme, has the same tRNA specificity as GluRS C; the other, called GluRS E, has eukaryotic (wheat germ) tRNA specificity. Both enzymes exhibit a molecular weight close to 160 000. Each of these enzymes co-eluate on hydroxyapatite and phosphocellulose chromatographies with an unstable active monomer whose molecular weight is approximately half that of the corresponding dimer. Two assumptions are discussed about these monomers.
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005975:Glutamate-tRNA Ligase / Q000302:isolation & purification*; D007526:Isoelectric Point; D008970:Molecular Weight; D010940:Plant Proteins / Q000302:isolation & purification; D014908:Triticum / Q000201:enzymology*
D010940:Plant Proteins; D000604:Amino Acyl-tRNA Synthetases; D005975:Glutamate-tRNA Ligase