| pubmed-article:6363389 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C0521346 | lld:lifeskim |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C2260131 | lld:lifeskim |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:6363389 | lifeskim:mentions | umls-concept:C1706536 | lld:lifeskim |
| pubmed-article:6363389 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6363389 | pubmed:dateCreated | 1984-3-23 | lld:pubmed |
| pubmed-article:6363389 | pubmed:abstractText | Expression of the glpA operon encoding the extrinsic membrane anaerobic sn-glycerol-3-phosphate dehydrogenase complex of Escherichia coli K-12 was studied in five strains carrying independent glpA-lac operon fusions. The location of the fusions was confirmed by transduction. Two of the strains produced an enzymatically active anaerobic sn-glycerol-3-phosphate dehydrogenase that accumulated in the cytoplasmic fraction of the cells. This suggests the loss of a specific membrane anchor subunit encoded by a distal gene, glpB, which was disrupted by the insertion. beta-Galactosidase in all five strains carrying phi(glpA-lac) was highly inducible by glycerol only anaerobically. A mutation in fnr, a pleiotropic activator gene, prevented full induction of the phi(glpA-lac), demonstrating that the Fnr protein is a positive regulator of the primary dehydrogenase as well as of the terminal reductases of anaerobic respiratory chains. Low concentrations of the respiratory poison KCN had a permissive effect on aerobic expression of phi(glpA-lac). Aerobic expression of the hybrid operon was also enhanced in isogenic derivatives of the fusion strains deficient in protoporphyrin biosynthesis (hemA). Thus, heme proteins may play a role in mediating aerobic repression of the anaerobic respiratory chain. | lld:pubmed |
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| pubmed-article:6363389 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6363389 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6363389 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6363389 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6363389 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:6363389 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:6363389 | pubmed:author | pubmed-author:LinE CEC | lld:pubmed |
| pubmed-article:6363389 | pubmed:author | pubmed-author:KuritzkesD... | lld:pubmed |
| pubmed-article:6363389 | pubmed:author | pubmed-author:ZhangX YXY | lld:pubmed |
| pubmed-article:6363389 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6363389 | pubmed:volume | 157 | lld:pubmed |
| pubmed-article:6363389 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6363389 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6363389 | pubmed:pagination | 591-8 | lld:pubmed |
| pubmed-article:6363389 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6363389 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6363389 | pubmed:articleTitle | Use of phi(glp-lac) in studies of respiratory regulation of the Escherichia coli anaerobic sn-glycerol-3-phosphate dehydrogenase genes (glpAB). | lld:pubmed |
| pubmed-article:6363389 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6363389 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:6363389 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6363389 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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