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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1988-8-11
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pubmed:abstractText |
The FNR protein of E. coli is a transcriptional activator required for the expression of genes involved in anaerobic respiratory pathways. Site-directed mutagenesis was used to alter three amino acids in the recognition helix of the putative DNA-binding domain of FNR, with the aim of changing its specificity to that of the cyclic AMP receptor protein (CRP). In the presence of the mutant protein (FNR-215) expression of the lac operon was activated during anaerobiosis and unaffected by glucose. FNR-215 did not have a uniform effect on the expression of other cAMP-CRP-dependent genes, but the results demonstrate the fundamental similarity between FNR- and CRP-mediated transcriptional activation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2838728-Amino Acid Sequence,
pubmed-meshheading:2838728-Anaerobiosis,
pubmed-meshheading:2838728-Bacterial Proteins,
pubmed-meshheading:2838728-Base Sequence,
pubmed-meshheading:2838728-Escherichia coli,
pubmed-meshheading:2838728-Gene Expression Regulation,
pubmed-meshheading:2838728-Genes,
pubmed-meshheading:2838728-Genes, Bacterial,
pubmed-meshheading:2838728-Lac Operon,
pubmed-meshheading:2838728-Molecular Sequence Data,
pubmed-meshheading:2838728-Mutation,
pubmed-meshheading:2838728-beta-Galactosidase
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pubmed:year |
1987
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pubmed:articleTitle |
Activation of the lac operon of Escherichia coli by a mutant FNR protein.
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pubmed:affiliation |
Department of Microbiology, University of Sheffield, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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