| Literature DB >> 737182 |
S Montasser Kouhsari, G Keith, J H Weil.
Abstract
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.Entities:
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Year: 1978 PMID： 737182 DOI： 10.1016/0005-2787(78)90299-x
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002