Source:http://linkedlifedata.com/resource/pubmed/id/15916606
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2005-5-26
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pubmed:abstractText |
The Bacillus subtilis ilv-leu operon involved in the biosynthesis of branched-chain amino acids is under negative regulation mediated by TnrA and CodY, which recognize and bind to their respective cis-elements located upstream of the ilv-leu promoter. This operon is known to be under CcpA-dependent positive regulation. We have currently identified a catabolite-responsive element (cre) for this positive regulation (bases -96 to -82; +1 is the ilv-leu transcription initiation base) by means of DNase I-footprinting in vitro, and deletion and base-substitution analyses of cre. Under nitrogen-rich growth conditions in glucose-minimal medium supplemented with glutamine and amino acids, CcpA and CodY exerted positive and negative regulation of ilv-leu, respectively, but TnrA did not function. Moreover, CcpA and CodY were able to function without their counteracting regulation of each other, although the CcpA-dependent positive regulation did not overcome the CodY-dependent negative regulation. Furthermore, under nitrogen-limited conditions in glucose-minimal medium with glutamate as the sole nitrogen source, CcpA and TnrA exerted positive and negative regulation, respectively, but CodY did not function. This CcpA-dependent positive regulation occurred without the TnrA-dependent negative regulation. However, the TnrA-dependent negative regulation did not occur without the CcpA-dependent positive regulation, raising the possibility that this negative regulation might decrease the CcpA-dependent positive regulation. The physiological role of this elaborate transcription regulation of the B. subtilis ilv-leu operon in overall metabolic regulation in this organism is discussed.
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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/Amino Acids, Branched-Chain,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoleucine,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ScgR protein, Bacillus subtilis,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Valine,
http://linkedlifedata.com/resource/pubmed/chemical/catabolite control proteins...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1560-73
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pubmed:dateRevised |
2009-7-17
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pubmed:meshHeading |
pubmed-meshheading:15916606-Amino Acids, Branched-Chain,
pubmed-meshheading:15916606-Bacillus subtilis,
pubmed-meshheading:15916606-Bacterial Proteins,
pubmed-meshheading:15916606-Base Sequence,
pubmed-meshheading:15916606-DNA Footprinting,
pubmed-meshheading:15916606-DNA-Binding Proteins,
pubmed-meshheading:15916606-Gene Expression Regulation, Bacterial,
pubmed-meshheading:15916606-Isoleucine,
pubmed-meshheading:15916606-Leucine,
pubmed-meshheading:15916606-Molecular Sequence Data,
pubmed-meshheading:15916606-Nitrogen,
pubmed-meshheading:15916606-Operon,
pubmed-meshheading:15916606-Repressor Proteins,
pubmed-meshheading:15916606-Response Elements,
pubmed-meshheading:15916606-Transcription, Genetic,
pubmed-meshheading:15916606-Transcription Factors,
pubmed-meshheading:15916606-Valine
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pubmed:year |
2005
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pubmed:articleTitle |
Elaborate transcription regulation of the Bacillus subtilis ilv-leu operon involved in the biosynthesis of branched-chain amino acids through global regulators of CcpA, CodY and TnrA.
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pubmed:affiliation |
Department of Biotechnology, Faculty of Life Science and Biotechnology, Fukuyama University, 985 Sanzo, Higashimura-cho, Fukuyama-shi, Hiroshima 729-0292, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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