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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1991-6-26
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pubmed:databankReference |
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pubmed:abstractText |
We have sequenced the fruR gene and flanking DNA fragments from Escherichia coli K12 and Salmonella typhimurium LT2. The fruR gene codes for a protein that represses the fru operon and activates the pps gene for PEP synthase. The corresponding open reading frame (ORF) FruR consists of 334 amino acid residues. The ORF contains an amino-terminal helix-turn-helix motif, characteristic of DNA-binding proteins and has similarity to known repressor proteins. The sequence is identical to that of the E. coli shl gene (mnemonic for suppressor-H-linked phenotype). It is flanked upstream by the ilvIH genes and downstream by the pbpB gene in both organisms and by orfB, a gene possibly involved in the regulation of cell division.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0026-8925
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
226
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
332-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1851954-Acetolactate Synthase,
pubmed-meshheading:1851954-Amino Acid Sequence,
pubmed-meshheading:1851954-Bacterial Proteins,
pubmed-meshheading:1851954-Base Sequence,
pubmed-meshheading:1851954-DNA, Bacterial,
pubmed-meshheading:1851954-Escherichia coli,
pubmed-meshheading:1851954-Escherichia coli Proteins,
pubmed-meshheading:1851954-Gene Expression Regulation, Bacterial,
pubmed-meshheading:1851954-Genes, Bacterial,
pubmed-meshheading:1851954-Molecular Sequence Data,
pubmed-meshheading:1851954-Phosphotransferases,
pubmed-meshheading:1851954-Phosphotransferases (Paired Acceptors),
pubmed-meshheading:1851954-Repressor Proteins,
pubmed-meshheading:1851954-Salmonella typhimurium
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pubmed:year |
1991
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pubmed:articleTitle |
Nucleotide sequence of the ilvH-fruR gene region of Escherichia coli K12 and Salmonella typhimurium LT2.
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pubmed:affiliation |
Fachbereich Biologie/Chemie, Universität Osnabrück, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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