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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1979-4-25
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
521
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
576-83
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:737182-Base Sequence,
pubmed-meshheading:737182-Chloroplasts,
pubmed-meshheading:737182-Methylation,
pubmed-meshheading:737182-Mitochondria,
pubmed-meshheading:737182-Nucleic Acid Conformation,
pubmed-meshheading:737182-Phenylalanine,
pubmed-meshheading:737182-Plants,
pubmed-meshheading:737182-RNA, Transfer,
pubmed-meshheading:737182-tRNA Methyltransferases
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pubmed:year |
1978
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pubmed:articleTitle |
Methylation of yeast tRNAPhe by enzymes from cytoplasm, chloroplasts and mitochondria of Phaseolus vulgaris.
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pubmed:publicationType |
Journal Article
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