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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2001-10-26
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pubmed:abstractText |
The 3'-terminal tRNA-like structure in turnip yellow mosaic virus (TYMV) RNA can be adenylated by tRNA nucleotidyltransferase and subsequently aminoacylated by valyl-tRNA synthetase. Here we present evidence that TYMV Val-RNA can form a stable complex with eukaryotic wheat germ elongation factor EF-1alpha and GTP: the Val-RNA is protected by EF-1alpha.. GTP against digestion by RNase A. By affinity chromatography of TYMV Val-RNA fragments on immobilized EF-1alpha . GTP, it has been established that the valylated aminoacyl RNA domain, which in TYMV RNA is formed by the 3' half of the tRNA-like region, is sufficient for complex formation with EF-1alpha . GTP. The aminoacyl RNA domain is equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T stem and loop. In line with these results, the aminoacyl RNA domain in TYMV Val-RNA complexed to EF-1 alpha . GTP is resistant to digestion by RNase A. It is also shown that the TYMV RNA replicase (RNA-dependent RNA polymerase) isolated from TYMV-infected Chinese cabbage leaves does not contain tRNA nucleotidyltransferase, valyl-tRNA synthetase or EF-1alpha. This suggests that interaction of TYMV RNA with EF-1alpha is not mandatory for replicase activity.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-16453415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-16453426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-16453568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-16617475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-179456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-2858851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4000923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4000943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4344282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4364433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4373529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4572945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4604127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-4820886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-5274462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-5921640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-598381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6176943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6285419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6370033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6472477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6556143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6559195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6765239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-6950195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-7035684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-7079175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-960575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11681331-978788
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1143-8
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:11681331-Base Sequence,
pubmed-meshheading:11681331-Escherichia coli,
pubmed-meshheading:11681331-Guanosine Triphosphate,
pubmed-meshheading:11681331-Molecular Sequence Data,
pubmed-meshheading:11681331-Peptide Elongation Factor 1,
pubmed-meshheading:11681331-RNA, Transfer, Amino Acyl,
pubmed-meshheading:11681331-RNA Replicase,
pubmed-meshheading:11681331-Substrate Specificity,
pubmed-meshheading:11681331-Tymovirus,
pubmed-meshheading:11681331-Valine-tRNA Ligase
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pubmed:year |
1986
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pubmed:articleTitle |
Interaction of turnip yellow mosaic virus Val-RNA with eukaryotic elongation factor EF-1 [alpha]. Search for a function.
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pubmed:affiliation |
Institut Jacques Monod, C.N.R.S. and Universite Paris VII, 2 Place Jussieu, 75251 Paris Cedex 05, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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