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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
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pubmed:dateCreated |
1992-11-23
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pubmed:databankReference | |
pubmed:abstractText |
Curli are thin, coiled, temperature-regulated fibres on fibronectin-binding Escherichia coli. The subunit protein of curli was highly homologous at its amino terminus to SEF-17, the subunit protein of thin, aggregative fimbriae of Salmonella enteritidis 27655 strain 3b, suggesting that these fibres form a novel class of surface organelles on enterobacteria. E. coli HB101 is non-curliated and unable to bind soluble, iodinated fibronectin. The phenotypically cryptic curlin subunit gene, csgA, in HB101 is transcriptionally activated by expressing the cytoplasmic Crl on a multicopy plasmid. Transcriptional activation of csgA by Crl was observed after growth at 26 degrees C but not at 37 degrees C, even though crl transcription was not thermoregulated. A deletion of the 39 carboxy-terminal residues abolished Crl activity, whereas a deletion of 10 residues at the C-terminus did not, implying that a region between residue 93 and 122 in the 132-amino-acid-residue large Crl protein is required for activating curli expression in E. coli HB101. crl is a normal housekeeping gene in E. coli and it is suggested that its gene product may either be a DNA-binding protein affecting chromatin structure as has been suggested for histone-like protein H1 or interact with specific regulatory protein(s) controlling transcription of genes required for curli formation and fibronectin binding.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Crl protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/csgA protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2443-52
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1357528-Amino Acid Sequence,
pubmed-meshheading:1357528-Bacterial Proteins,
pubmed-meshheading:1357528-Base Sequence,
pubmed-meshheading:1357528-Escherichia coli,
pubmed-meshheading:1357528-Escherichia coli Proteins,
pubmed-meshheading:1357528-Fibronectins,
pubmed-meshheading:1357528-Fimbriae, Bacterial,
pubmed-meshheading:1357528-Gene Expression Regulation, Bacterial,
pubmed-meshheading:1357528-Genes, Bacterial,
pubmed-meshheading:1357528-Hot Temperature,
pubmed-meshheading:1357528-Molecular Sequence Data,
pubmed-meshheading:1357528-Organelles,
pubmed-meshheading:1357528-Transcription, Genetic
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pubmed:year |
1992
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pubmed:articleTitle |
The Crl protein activates cryptic genes for curli formation and fibronectin binding in Escherichia coli HB101.
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pubmed:affiliation |
Department of Microbiology, University of Umeå, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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