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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1980-7-26
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pubmed:abstractText |
The protein synthesis elongation factor EF-Tu, complexed with EF-Ts, forms part of Q beta RNA replicase. In an effort to determine its function in the RNA synthesis reaction, we have developed procedures which allow us to replace the endogenous EF-Tu in purified Q beta replicase with EF-Tu from a variety of sources. In this communication we report purification of EF-Tu from strains containing (a) a wild type tufA gene only, (b) a kirromycin-resistant mutant tufA gene only, and (c) a kirromycin-resistant mutant tufA gene and a mutant tufB gene which codes for EF-Tu that does not bind ribosomes. When each of these EF-Tu preparations is inserted in Q beta replicase, the wild type tufA gene product and and the tufB gene product function appearently normally, but the kirromycin-resistant tufA gene product causes the formation of an altered enzyme. The Q beta replicase containing kirromycin-resistant EF-Tu is unstable; it is rapidly inactivated in the reaction mixture, even at temperatures as low as 20 degrees C. This property results in an apparent increase in template specificity; while wild type Q beta replicase will transcribe poly(C) and other synthetic RNA species, the mutant enzyme will do so only in the presence of Mn2+, which reduces template specificity. The kirromycin-resistant Q beta replicase will also transcribe Q beta RNA. The results imply that EF-Tu is involved in maintenance of enzyme structure, which, in turn, is implicated in template specificity.
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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/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridones,
http://linkedlifedata.com/resource/pubmed/chemical/Q beta Replicase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/mocimycin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
255
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5300-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6989824-Anti-Bacterial Agents,
pubmed-meshheading:6989824-Escherichia coli,
pubmed-meshheading:6989824-Genes,
pubmed-meshheading:6989824-Kinetics,
pubmed-meshheading:6989824-Magnesium,
pubmed-meshheading:6989824-Manganese,
pubmed-meshheading:6989824-Mutation,
pubmed-meshheading:6989824-Peptide Elongation Factors,
pubmed-meshheading:6989824-Pyridones,
pubmed-meshheading:6989824-Q beta Replicase,
pubmed-meshheading:6989824-RNA Nucleotidyltransferases,
pubmed-meshheading:6989824-Species Specificity
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pubmed:year |
1980
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pubmed:articleTitle |
Q beta replicase containing wild type and mutant tufA and tufB gene.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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