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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2002-9-26
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pubmed:abstractText |
The mosquitocidal toxin (MTX) produced by Bacillus sphaericus strain SSII-1 is an approximately 97-kDa single-chain toxin which contains a 27-kDa enzyme domain harboring ADP-ribosyltransferase activity and a 70-kDa putative binding domain. Due to cytotoxicity toward bacterial cells, the 27-kDa enzyme fragment cannot be produced in Escherichia coli expression systems. However, a nontoxic 32-kDa N-terminal truncation of MTX can be expressed in E. coli and subsequently cleaved to an active 27-kDa enzyme fragment. In vitro the 27-kDa enzyme fragment of MTX ADP-ribosylated numerous proteins in E. coli lysates, with dominant labeling of an approximately 45-kDa protein. Matrix-assisted laser desorption ionization-time-of-flight mass spectrometry combined with peptide mapping identified this protein as the E. coli elongation factor Tu (EF-Tu). ADP ribosylation of purified EF-Tu prevented the formation of the stable ternary EF-Tuaminoacyl-tRNAGTP complex, whereas the binding of GTP to EF-Tu was not altered. The inactivation of EF-Tu by MTX-mediated ADP-ribosylation and the resulting inhibition of bacterial protein synthesis are likely to play important roles in the cytotoxicity of the 27-kDa enzyme fragment of MTX toward E. coli.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-11124969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-11772013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-11812773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-11821389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-1573997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-1901061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-208069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-2493391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-2498316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-2498323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-2891567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-3122025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-3140813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-3223989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-3335520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-3863818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-3934172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-7000782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-729585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-7548001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-7713889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-7918447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-8096838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-8460141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12324336-9516428
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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 |
Oct
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pubmed:issn |
0099-2240
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
68
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4894-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12324336-Adenosine Diphosphate Ribose,
pubmed-meshheading:12324336-Bacillus,
pubmed-meshheading:12324336-Bacterial Toxins,
pubmed-meshheading:12324336-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12324336-Escherichia coli,
pubmed-meshheading:12324336-Mutation,
pubmed-meshheading:12324336-Peptide Elongation Factor Tu,
pubmed-meshheading:12324336-Peptide Fragments,
pubmed-meshheading:12324336-Plasmids,
pubmed-meshheading:12324336-Protein Binding,
pubmed-meshheading:12324336-Recombinant Fusion Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylation.
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pubmed:affiliation |
Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, D-79104 Freiburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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