| pubmed-article:10828971 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0003284 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0012408 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C1537998 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:10828971 | lifeskim:mentions | umls-concept:C0046917 | lld:lifeskim |
| pubmed-article:10828971 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:10828971 | pubmed:dateCreated | 2000-7-11 | lld:pubmed |
| pubmed-article:10828971 | pubmed:abstractText | Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase (DMAPP-tRNA transferase) catalyzes the alkylation of the exocyclic amine of A37 by a dimethylallyl unit in tRNAs with an adenosine in the third anticodon position (position 36). By use of purified recombinant enzyme, steady- state kinetic studies were conducted with chemically synthesized RNA oligoribonucleotides to determine the essential elements within the tRNA anticodon stem-loop structure required for recognition by the enzyme. A 17-base oligoribonucleotide corresponding to the anticodon stem-loop of E. coli tRNA(Phe) formed a stem-loop minihelix (minihelix(Phe)) when annealed rapidly on ice, while the same molecule formed a duplex structure with a central loop when annealed slowly at higher concentrations. Both the minihelix and duplex structures gave k(cat)s similar to that for the normal substrate (full-length tRNA(Phe) unmodified at A37), although the K(m) for minihelix(Phe) was approximately 180-fold higher than full-length tRNA. The A36-A37-A38 motif, which is completely conserved in tRNAs modified by the enzyme, was found to be important for modification. Changing A36 to G in the minihelix resulted in a 260-fold reduction in k(cat) compared to minihelix(Phe) and a 13-fold increase in K(m). An A38G variant was modified with a 9-fold reduction in k(cat) and a 5-fold increase in K(m). A random coil 17-base oligoribonucleotide in which the loop sequence of E. coli tRNA(Phe) was preserved, but the 5 base pair helix stem was completely disrupted and showed no measurable activity, indicating that a helix-loop structure is essential for recognition. Finally, altering the identity of several base pairs in the helical stem did not have a major effect on catalytic efficiency, suggesting that the enzyme does not make base-specific contacts important for binding or catalysis in this region. | lld:pubmed |
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| pubmed-article:10828971 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10828971 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10828971 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10828971 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10828971 | pubmed:month | May | lld:pubmed |
| pubmed-article:10828971 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10828971 | pubmed:author | pubmed-author:PoulterC DCD | lld:pubmed |
| pubmed-article:10828971 | pubmed:author | pubmed-author:SoderbergTT | lld:pubmed |
| pubmed-article:10828971 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10828971 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:10828971 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:10828971 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10828971 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10828971 | pubmed:pagination | 6546-53 | lld:pubmed |
| pubmed-article:10828971 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10828971 | pubmed:meshHeading | pubmed-meshheading:10828971... | lld:pubmed |
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| pubmed-article:10828971 | pubmed:meshHeading | pubmed-meshheading:10828971... | lld:pubmed |
| pubmed-article:10828971 | pubmed:meshHeading | pubmed-meshheading:10828971... | lld:pubmed |
| pubmed-article:10828971 | pubmed:meshHeading | pubmed-meshheading:10828971... | lld:pubmed |
| pubmed-article:10828971 | pubmed:meshHeading | pubmed-meshheading:10828971... | lld:pubmed |
| pubmed-article:10828971 | pubmed:meshHeading | pubmed-meshheading:10828971... | lld:pubmed |
| pubmed-article:10828971 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10828971 | pubmed:articleTitle | Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop. | lld:pubmed |
| pubmed-article:10828971 | pubmed:affiliation | Department of Chemistry, University of Utah, Salt Lake City 84112, USA. | lld:pubmed |
| pubmed-article:10828971 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10828971 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:948690 | entrezgene:pubmed | pubmed-article:10828971 | lld:entrezgene |
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