Methylation of yeast tRNAPhe by enzymes from cytoplasm, chloroplasts and mitochondria of Phaseolus vulgaris.
Pure yeast tRNAPhe was used as a substrate to compare the tRNA methylating activities in Phaseolus vulgaris cytoplasm, chloroplasts and mitochondria, in the presence of S-adenosyl[Me-3H]methionine. The resulting [Me-3H]-tRNAPhe was then analyzed, using the techniques of nucleotide sequence determination. Cytoplasmic and mitochondrial enzymes catalyze the methylation (into m5C) of C48 present in the extra-loop, while chloroplast enzyme preparations catalyze the modification (into m1A) of A14 present in the dihydrouridine loop of tRNAPhe.
D001483:Base Sequence; D002736:Chloroplasts / Q000201:enzymology*; D008745:Methylation; D008928:Mitochondria / Q000201:enzymology*; D009690:Nucleic Acid Conformation; D010649:Phenylalanine; D010944:Plants; D012343:RNA, Transfer / Q000378:metabolism*; D012359:tRNA Methyltransferases / Q000378:metabolism*
D010649:Phenylalanine; D012343:RNA, Transfer; D012359:tRNA Methyltransferases