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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
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pubmed:dateCreated |
1993-7-13
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pubmed:abstractText |
We have previously reported that the thiols glutathione, dithiothreitol, and beta-mercaptoethanol suppress transcription of the Escherichia coli manganese-containing superoxide dismutase gene (sodA) in an in vitro coupled transcription plus translation system (Gardner, P. R., and Fridovich, I. (1987) J. Biol. Chem. 262, 17591-17595). We now report that NADPH, but not NADH, selectively decreases transcription of sodA in vitro and that an NADPH generating system utilizing glucose 6-phosphate and the corresponding dehydrogenase markedly augments this suppressive effect. A redox buffer containing various ratios of oxidized and reduced glutathione also modulated transcription of sodA thus demonstrating the existence of a redox-sensitive mechanism controlling sodA transcription. Fusion of a 120-base pair fragment, containing 90 base pairs of DNA upstream of the sodA transcription initiation site, to a promoterless galactokinase gene (galK) conferred redox-sensitivity to GalK synthesis. We propose that these redox effects act through a redox-sensitive regulator of sodA and that the anabolic reduction charge, [NADPH]/([NADPH]+[NADP+]), is one cellular signal controlling sodA transcription.
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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/Galactokinase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Disulfide,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase
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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 |
15
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pubmed:volume |
268
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pubmed:geneSymbol |
galK,
nfo,
sodA,
zwf
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12958-63
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8509428-Base Sequence,
pubmed-meshheading:8509428-Escherichia coli,
pubmed-meshheading:8509428-Galactokinase,
pubmed-meshheading:8509428-Gene Expression Regulation, Bacterial,
pubmed-meshheading:8509428-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8509428-Genes, Bacterial,
pubmed-meshheading:8509428-Glutathione,
pubmed-meshheading:8509428-Glutathione Disulfide,
pubmed-meshheading:8509428-Kinetics,
pubmed-meshheading:8509428-Molecular Sequence Data,
pubmed-meshheading:8509428-NAD,
pubmed-meshheading:8509428-NADP,
pubmed-meshheading:8509428-Oxidation-Reduction,
pubmed-meshheading:8509428-Promoter Regions, Genetic,
pubmed-meshheading:8509428-Protein Biosynthesis,
pubmed-meshheading:8509428-RNA, Messenger,
pubmed-meshheading:8509428-Sequence Homology, Nucleic Acid,
pubmed-meshheading:8509428-Superoxide Dismutase,
pubmed-meshheading:8509428-Transcription, Genetic
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pubmed:year |
1993
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pubmed:articleTitle |
NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro.
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pubmed:affiliation |
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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