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rdf:type |
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lifeskim:mentions |
umls-concept:C0003284,
umls-concept:C0020792,
umls-concept:C0030054,
umls-concept:C0035553,
umls-concept:C0035711,
umls-concept:C0205369,
umls-concept:C1167622,
umls-concept:C1514873,
umls-concept:C1537998,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
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pubmed:issue |
24
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pubmed:dateCreated |
1998-1-8
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pubmed:abstractText |
tRNA binding to the ribosomal P site is dependent not only on correct codon-anticodon interaction but also involves identification of structural elements of tRNA by the ribosome. By using a phosphorothioate substitution-interference approach, we identified specific nonbridging Rp-phosphate oxygens in the anticodon loop of tRNA(Phe) from Escherichia coli which are required for P-site binding. Stereospecific involvement of phosphate oxygens at these positions was confirmed by using synthetic anticodon arm analogues at which single Rp- or Sp-phosphorothioates were incorporated. Identical interference results with yeast tRNA(Phe) and E. coli tRNA(fMet) indicate a common backbone conformation or common recognition elements in the anticodon loop of tRNAs. N-ethyl-N-nitrosourea modification-interference experiments with natural tRNAs point to the importance of the same phosphates in the loop. Guided by the crystal structure of tRNA(Phe), we propose that specific Rp-phosphate oxygens are required for anticodon loop ("U-turn") stabilization or are involved in interactions with the ribosome on correct tRNA-mRNA complex formation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-1381501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-1701151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-1709484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-1870974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-1883196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-221915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-23826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-2405162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-2411211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-2438652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-2690016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-3071687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-3277187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-4352931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-460419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-6334536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-6345793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7002606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7042337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7048255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7528943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7566085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7585250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7588616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7629066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7657623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7683490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7688564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-782513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-790568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7973729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-7982992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-8049279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-8194535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-8265362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371759-8990398
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Anticodon,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylnitrosourea,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Met,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Phe,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12823-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9371759-Anticodon,
pubmed-meshheading:9371759-Binding Sites,
pubmed-meshheading:9371759-Escherichia coli,
pubmed-meshheading:9371759-Ethylnitrosourea,
pubmed-meshheading:9371759-Oxygen,
pubmed-meshheading:9371759-RNA, Transfer, Met,
pubmed-meshheading:9371759-RNA, Transfer, Phe,
pubmed-meshheading:9371759-Ribosomal Proteins,
pubmed-meshheading:9371759-Ribosomes,
pubmed-meshheading:9371759-Saccharomyces cerevisiae,
pubmed-meshheading:9371759-Thionucleotides
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pubmed:year |
1997
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pubmed:articleTitle |
Identification of specific Rp-phosphate oxygens in the tRNA anticodon loop required for ribosomal P-site binding.
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pubmed:affiliation |
Institute of Microbiology and Genetics, University of Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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