rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
23
|
pubmed:dateCreated |
1981-4-13
|
pubmed:abstractText |
The requirements for the decoding process at the ribosomal A site have been investigated in the presence of viomycin. For these studies natural mRNA was replaced either by the synthetic oligonucleotide A-U-G(-U)n, with 0 less than or equal to n less than or equal to 4, or by a physical mixture of the oligonucleotides A-U-G and various oligo(U) sequences. Thus the effect of the "removal" of selected covalent bonds from the sequence A-U-G(U)n could be studied. When the ribosomal P site contains tRNAMetf, then normally the full hexanucleotide "messenger" A-U-G-U-U-U is needed for the EF-Tu-mediated binding of Phe-tRNA into the A site. However in presence of viomycin the pentanucleotide A-U-G-U-U suffices for this. It is also possible in the presence of viomycin to replace A-U-G-U and U-U. In all the above systems the binding of Phe-tRNA required the presence of EF-Tu and GTP. The results suggest that viomycin reinforces interactions between aa-tRNA and the A site after the codon-anticodon recognition step.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-14172630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-16591528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-183772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-202460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-209306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-212033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4559253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4563073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4575689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4580677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4589304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-460419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4902886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4902905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-4945116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6162154-6243944
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anticodon,
http://linkedlifedata.com/resource/pubmed/chemical/Codon,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligoribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/Viomycin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
0305-1048
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
11
|
pubmed:volume |
8
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5813-24
|
pubmed:dateRevised |
2010-9-13
|
pubmed:meshHeading |
pubmed-meshheading:6162154-Anticodon,
pubmed-meshheading:6162154-Binding Sites,
pubmed-meshheading:6162154-Codon,
pubmed-meshheading:6162154-Dipeptides,
pubmed-meshheading:6162154-Escherichia coli,
pubmed-meshheading:6162154-Oligoribonucleotides,
pubmed-meshheading:6162154-RNA, Bacterial,
pubmed-meshheading:6162154-RNA, Messenger,
pubmed-meshheading:6162154-RNA, Transfer,
pubmed-meshheading:6162154-RNA, Transfer, Amino Acyl,
pubmed-meshheading:6162154-Ribosomes,
pubmed-meshheading:6162154-Viomycin
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pubmed:year |
1980
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pubmed:articleTitle |
Dinucleotide codon-anticodon interaction as a minimum requirement for ribosomal aa-tRNA binding: stabilisation by viomycin of aa-tRNA in the A site.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|