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- W2007226009 abstract "Transfer RNAs and aminoacyl-tRNA synthetases of phenylalanine, tyrosine and tryptophan were localized in the cytoplasm, the chloroplasts and in the mitochondria. The aminoacyl-tRNA synthetases of these three aromatic amino acids fractionated by hydroxylapatite chromatography from both chloroplasts and mitochondria were able to aminoacylate Escherichia coli tRNA suggesting their prokaryotic nature. On the other hand, cytoplasmic enzymes were unable to aminoacylate E. coli tRNA and they were found to be distinct from the organellar aminoacyl-tRNA synthetases in chromatographic behaviour as well as in their kinetic properties. Three isoacceptors for each of tRNAPhe and tRNATrp were resolved by reversed phase chromatography (RPC-5) and one isoacceptor was localized in each for cytoplasm, chloroplasts and mitochondria. tRNATyr was resolved into 5 isoacceptors; 2 were localized in cytoplasm, 2 in chloroplasts and the remaining 1 in mitochondria. Organellar tRNAs in all the three cases could be aminoacylated by E. coli aminoacyl-tRNA synthetases while cytoplasmic tRNAs were not aminoacylatable by E. coli enzymes. Codon recognition studies with tRNATyr isoacceptors indicated that all the organellar isoacceptors recognize UAC codon whereas one of the cytoplasmic isoacceptors recognizes UAC codon and the other recognized UAU codon." @default.
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- W2007226009 date "1982-04-01" @default.
- W2007226009 modified "2023-09-24" @default.
- W2007226009 title "Characterization of Glycine max cytoplasmic, chloroplastic and mitochondrial tRNAs and synthetases for phenylalanine, tryptophan and tyrosine" @default.
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- W2007226009 doi "https://doi.org/10.1016/0304-4211(82)90209-7" @default.
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