| pubmed-article:7011814 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7011814 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:7011814 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
| pubmed-article:7011814 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:7011814 | lifeskim:mentions | umls-concept:C1537998 | lld:lifeskim |
| pubmed-article:7011814 | lifeskim:mentions | umls-concept:C0073347 | lld:lifeskim |
| pubmed-article:7011814 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7011814 | pubmed:dateCreated | 1981-6-25 | lld:pubmed |
| pubmed-article:7011814 | 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. | lld:pubmed |
| pubmed-article:7011814 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7011814 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7011814 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7011814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7011814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7011814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7011814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7011814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7011814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7011814 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7011814 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7011814 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:7011814 | pubmed:author | pubmed-author:AlbaniMM | lld:pubmed |
| pubmed-article:7011814 | pubmed:author | pubmed-author:NierhausK HKH | lld:pubmed |
| pubmed-article:7011814 | pubmed:author | pubmed-author:KerstenHH | lld:pubmed |
| pubmed-article:7011814 | pubmed:author | pubmed-author:WurmbachPP | lld:pubmed |
| pubmed-article:7011814 | pubmed:author | pubmed-author:MännleinEE | lld:pubmed |
| pubmed-article:7011814 | pubmed:author | pubmed-author:PraislerRR | lld:pubmed |
| pubmed-article:7011814 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7011814 | pubmed:volume | 114 | lld:pubmed |
| pubmed-article:7011814 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7011814 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7011814 | pubmed:pagination | 451-6 | lld:pubmed |
| pubmed-article:7011814 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:meshHeading | pubmed-meshheading:7011814-... | lld:pubmed |
| pubmed-article:7011814 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:7011814 | pubmed:articleTitle | On the role of ribosylthymine in prokaryotic tRNA function. | lld:pubmed |
| pubmed-article:7011814 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7011814 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7011814 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7011814 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7011814 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7011814 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7011814 | lld:pubmed |
