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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1978-12-2
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pubmed:abstractText |
Bulk tRNA from yeast and Rat liver can be methylated in vitro with -adenosylmethionine and B, subtilis extracts. The sole product formed is 1-methyladenosine (m1A). This tRNA (adenine-1) methyltransferase converts quantitatively the 3'-terminal adenosine-residue in the dihydrouridine-loop of tRNAThr and tRNATyr from yeast into m1A. Out of 16 eucaryotic tRNAs with known sequences 6 accepted methyl groups, all at a molar ratio of 1. These tRNAs have in common an unpaired adenosine-residue at the specific site in the sequence Py-A-A+-G-G-C-m2G. Out of 12 tRNAs from E. coli 6 served as specific substrates. These E. coli tRNAs also have an unpaired adenosine-residue at the 3'-end of the D-loop. Besides restrictions in primary structure intact secondary and tertiary structure is important for recognition of the specific tRNAs by the enzyme.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-10793703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-343782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-347399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-408794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-4201118,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-4555033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-4563428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-4596141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-4604768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-4632322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-5327073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-5582428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-629973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-782517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-782564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-820377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/99729-927512
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3033-42
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:99729-Bacillus subtilis,
pubmed-meshheading:99729-Base Sequence,
pubmed-meshheading:99729-Eukaryotic Cells,
pubmed-meshheading:99729-Methylation,
pubmed-meshheading:99729-Nucleic Acid Conformation,
pubmed-meshheading:99729-Nucleic Acid Denaturation,
pubmed-meshheading:99729-Prokaryotic Cells,
pubmed-meshheading:99729-RNA, Transfer,
pubmed-meshheading:99729-Structure-Activity Relationship,
pubmed-meshheading:99729-Substrate Specificity,
pubmed-meshheading:99729-tRNA Methyltransferases
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pubmed:year |
1978
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pubmed:articleTitle |
Recognition of individual procaryotic and eucaryotic transfer-ribonucleic acids by B subtilis adenine-1-methyltransferase specific for the dihydrouridine loop.
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pubmed:publicationType |
Journal Article
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