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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1981-6-25
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pubmed:abstractText |
tRNAPhe and tRNALys were isolated from an Escherichia coli K12 mutant deficient in ribosylthymine (rT) and from the wild-type strain. The sequence G-rT-psi-C which is common to loop IV of practically all tRNAs used in the elongation cycle of protein synthesis reads G-U-psi-C in the tRNAs of the mutant strain. The purified tRNAs were compared in various steps of protein biosynthesis. The poly(U)-dependent poly(Phe) synthesis performed with purified Phe-tRNAPhe and purified elongation factors showed no dependence on the presence or absence of ribosylthymine in the respective tRNAs. In contrast, the corresponding poly(A)-dependent poly(Lys) synthesis was markedly increased when Lys-tRNALys lacking rT was used. The analysis of individual functional steps of the poly(A)-dependent elongation cycle demonstrated that the absence of rT reduced the binding to the A-site and improved the translocation reaction, whereas the formation of the ternary complex EF-Tu . GTP . aa-tRNA as well as both tRNA binding to the P-site and the peptidyltransferase reaction remained unaffected. The presence of U in place of rT in tRNA increases the misincorporation of leucine in an optimized poly(U)/poly(Phe) system from about 3 in 10 000 to 3 in 1000. Our results are in agreement with the view that rT is involved in tRNA binding to the A-site in contrast to the P-site, and suggested that the presence of rT in tRNA improves the fidelity of the decoding process at the A-site of the ribosome.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor Tu,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine,
http://linkedlifedata.com/resource/pubmed/chemical/ribothymidine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
114
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
451-6
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:7011814-Bacterial Proteins,
pubmed-meshheading:7011814-Base Sequence,
pubmed-meshheading:7011814-Escherichia coli,
pubmed-meshheading:7011814-Kinetics,
pubmed-meshheading:7011814-Mutation,
pubmed-meshheading:7011814-Peptide Chain Elongation, Translational,
pubmed-meshheading:7011814-Peptide Elongation Factor Tu,
pubmed-meshheading:7011814-Poly A,
pubmed-meshheading:7011814-Protein Biosynthesis,
pubmed-meshheading:7011814-RNA, Transfer,
pubmed-meshheading:7011814-Ribosomes,
pubmed-meshheading:7011814-Uridine
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pubmed:year |
1981
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pubmed:articleTitle |
On the role of ribosylthymine in prokaryotic tRNA function.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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