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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5725
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pubmed:dateCreated |
2005-5-20
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pubmed:abstractText |
During transfer RNA (tRNA) selection, a cognate codon:anticodon interaction triggers a series of events that ultimately results in the acceptance of that tRNA into the ribosome for peptide-bond formation. High-fidelity discrimination between the cognate tRNA and near- and noncognate ones depends both on their differential dissociation rates from the ribosome and on specific acceleration of forward rate constants by cognate species. Here we show that a mutant tRNA(Trp) carrying a single substitution in its D-arm achieves elevated levels of miscoding by accelerating these forward rate constants independent of codon:anticodon pairing in the decoding center. These data provide evidence for a direct role for tRNA in signaling its own acceptance during decoding and support its fundamental role during the evolution of protein synthesis.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-10393195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-10677222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-10721991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-1101224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-11283358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-11340196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-11497425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-1182215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-12379845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-12464183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-12963376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-14566331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-14759365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-15475967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-15905389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-16590179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-2455872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-2469803,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-341160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-383994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-4530290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15905403-4933412
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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/Codon,
http://linkedlifedata.com/resource/pubmed/chemical/Codon, Terminator,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor Tu,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Trp
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
308
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1178-80
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pubmed:dateRevised |
2010-9-15
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pubmed:meshHeading |
pubmed-meshheading:15905403-Anticodon,
pubmed-meshheading:15905403-Base Pairing,
pubmed-meshheading:15905403-Codon,
pubmed-meshheading:15905403-Codon, Terminator,
pubmed-meshheading:15905403-Dipeptides,
pubmed-meshheading:15905403-GTP Phosphohydrolases,
pubmed-meshheading:15905403-Guanosine Triphosphate,
pubmed-meshheading:15905403-Hydrolysis,
pubmed-meshheading:15905403-Kinetics,
pubmed-meshheading:15905403-Mutation,
pubmed-meshheading:15905403-Nucleic Acid Conformation,
pubmed-meshheading:15905403-Peptide Elongation Factor Tu,
pubmed-meshheading:15905403-Protein Biosynthesis,
pubmed-meshheading:15905403-RNA, Messenger,
pubmed-meshheading:15905403-RNA, Transfer, Trp,
pubmed-meshheading:15905403-Ribosomes
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pubmed:year |
2005
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pubmed:articleTitle |
An active role for tRNA in decoding beyond codon:anticodon pairing.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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