Source:http://linkedlifedata.com/resource/pubmed/id/19956942
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2010-3-18
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pubmed:abstractText |
We found that penicillin-induced glutamate production by Corynebacterium glutamicum is inhibited when a de novo protein synthesis inhibitor, chloramphenicol, is added simultaneously with penicillin. When chloramphenicol was added 4 h after penicillin addition, glutamate production was essentially unaffected. (3)H-Leucine incorporation experiments revealed that protein synthesis continued for 1 h after penicillin addition and then gradually decreased. These results suggest that de novo protein synthesis within 4 h of penicillin treatment is required for the induction of glutamate production. To identify the protein(s) necessary for penicillin-induced glutamate production, proteome analysis of penicillin-treated C. glutamicum cells was performed with two-dimensional gel electrophoresis. Of more than 500 proteins detected, the amount of 13 proteins, including OdhI (an inhibitory protein for 2-oxoglutarate dehydrogenase complex), significantly increased upon penicillin treatment. Artificial overexpression of the odhI gene resulted in the decreased specific activity of the 2-oxoglutarate dehydrogenase complex and increased glutamate production without any triggers. These results suggest that the de novo synthesis of OdhI is the necessary factor for penicillin-induced glutamate overproduction by C. glutamicum. Moreover, continuous glutamate production was achieved by overexpression of odhI without any triggers. Thus, the odhI-overexpressing strain of C. glutamicum can be useful for efficient glutamate production.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteome,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1432-0614
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
911-20
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pubmed:meshHeading |
pubmed-meshheading:19956942-Anti-Bacterial Agents,
pubmed-meshheading:19956942-Bacterial Proteins,
pubmed-meshheading:19956942-Chloramphenicol,
pubmed-meshheading:19956942-Corynebacterium glutamicum,
pubmed-meshheading:19956942-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:19956942-Gene Expression,
pubmed-meshheading:19956942-Glutamic Acid,
pubmed-meshheading:19956942-Penicillins,
pubmed-meshheading:19956942-Proteome,
pubmed-meshheading:19956942-Staining and Labeling,
pubmed-meshheading:19956942-Transcriptional Activation,
pubmed-meshheading:19956942-Tritium
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pubmed:year |
2010
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pubmed:articleTitle |
Requirement of de novo synthesis of the OdhI protein in penicillin-induced glutamate production by Corynebacterium glutamicum.
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pubmed:affiliation |
Department of Biotechnology, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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