pubmed-article:4156359 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0001699 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0017801 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0028174 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0028161 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
pubmed-article:4156359 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
pubmed-article:4156359 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:4156359 | pubmed:dateCreated | 1975-6-21 | lld:pubmed |
pubmed-article:4156359 | pubmed:abstractText | Mutations causing constitutive synthesis of glutamine synthetase (GlnC(-) phenotype) were transferred from Klebsiella aerogenes into Klebsiella pneumoniae by P1-mediated transduction. Such GlnC(-) strains of K. pneumoniae have constitutive levels of glutamine synthetase. Two of three GlnC(-) strains of K. pneumoniae studied, each containing independently isolated mutations that confer the GlnC(-) phenotype, continue to synthesize nitrogenase in the presence of NH(4) (+). One strain, KP5069, produces 30% as much nitrogenase when grown in the presence of 15 mM NH(4) (+) as in its absence. The GlnC(-) phenotype allows the synthesis of nitrogenase to continue under conditions that completely repress nitrogenase synthesis in the wild-type strain. Glutamine auxotrophs of K. pneumoniae, that do not produce catalytically active glutamine synthetase, are unable to synthesize nitrogenase during nitrogen limited growth. Complementation of K. pneumoniae Gln(-) strains by an Escherichia coli episome (F'133) simultaneously restores glutamine synthetase activity and the ability to synthesize nitrogenase. These results indicate a role for glutamine synthetase as a positive control element for nitrogen fixation in K. pneumoniae. | lld:pubmed |
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pubmed-article:4156359 | pubmed:language | eng | lld:pubmed |
pubmed-article:4156359 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4156359 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:4156359 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:4156359 | pubmed:month | Nov | lld:pubmed |
pubmed-article:4156359 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:4156359 | pubmed:author | pubmed-author:MorandiCC | lld:pubmed |
pubmed-article:4156359 | pubmed:author | pubmed-author:ShanmugamK... | lld:pubmed |
pubmed-article:4156359 | pubmed:author | pubmed-author:GoldbergR BRB | lld:pubmed |
pubmed-article:4156359 | pubmed:author | pubmed-author:StreicherS... | lld:pubmed |
pubmed-article:4156359 | pubmed:author | pubmed-author:AusubelFF | lld:pubmed |
pubmed-article:4156359 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:4156359 | pubmed:volume | 120 | lld:pubmed |
pubmed-article:4156359 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:4156359 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:4156359 | pubmed:pagination | 815-21 | lld:pubmed |
pubmed-article:4156359 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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pubmed-article:4156359 | pubmed:year | 1974 | lld:pubmed |
pubmed-article:4156359 | pubmed:articleTitle | Regulation of nitrogen fixation in Klebsiella pneumoniae: evidence for a role of glutamine synthetase as a regulator of nitrogenase synthesis. | lld:pubmed |
pubmed-article:4156359 | pubmed:publicationType | Journal Article | lld:pubmed |
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