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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2002-12-19
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pubmed:abstractText |
Caenorhabditis elegans mitochondria have two elongation factor (EF)-Tu species, denoted EF-Tu1 and EF-Tu2. Recombinant nematode EF-Ts purified from Escherichia coli bound both of these molecules and also stimulated the translational activity of EF-Tu, indicating that the nematode EF-Ts homolog is a functional EF-Ts protein of mitochondria. Complexes formed by the interaction of nematode EF-Ts with EF-Tu1 and EF-Tu2 could be detected by native gel electrophoresis and purified by gel filtration. Although the nematode mitochondrial (mt) EF-Tu molecules are extremely unstable and easily form aggregates, native gel electrophoresis and gel filtration analysis revealed that EF-Tu.EF-Ts complexes are significantly more soluble. This indicates that nematode EF-Ts can be used to stabilize homologous EF-Tu molecules for experimental purposes. The EF-Ts bound to two eubacterial EF-Tu species (E.coli and Thermus thermophilus). Although the EF-Ts did not bind to bovine mt EF-Tu, it could bind to a chimeric nematode-bovine EF-Tu molecule containing domains 1 and 2 from bovine mt EF-Tu. Thus, the nematode EF-Ts appears to have a broad specificity for EF-Tu molecules from different species.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-10801827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-11262399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-11456491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-11772013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-11904178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-12145639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-1551572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-2199796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-2250005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-2808417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-330227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-367783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-4040515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-5432207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-7615523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-8077242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-8547323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-8596629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-8965699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-9048878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-9177488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-9253415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-9256058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-9268331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-9644241,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12490713-9774433
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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 |
Dec
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5444-51
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12490713-Animals,
pubmed-meshheading:12490713-Binding, Competitive,
pubmed-meshheading:12490713-Caenorhabditis elegans,
pubmed-meshheading:12490713-Cattle,
pubmed-meshheading:12490713-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12490713-Escherichia coli,
pubmed-meshheading:12490713-Gene Expression,
pubmed-meshheading:12490713-Guanosine Diphosphate,
pubmed-meshheading:12490713-Mitochondria,
pubmed-meshheading:12490713-Peptide Elongation Factor Tu,
pubmed-meshheading:12490713-Peptide Elongation Factors,
pubmed-meshheading:12490713-Protein Binding,
pubmed-meshheading:12490713-Recombinant Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Characterization of the interaction between the nucleotide exchange factor EF-Ts from nematode mitochondria and elongation factor Tu.
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pubmed:affiliation |
Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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