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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1991-7-19
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pubmed:abstractText |
The shape of the flagellar filaments of the bacterium Salmonella typhimurium under ordinary conditions is a left-handed helix. In addition to the normal wild-type filament, non-helical (i.e. straight), right-handed helical (early), or circular (semi-coiled and coiled) filaments and filament with small amplitude (fl-type) have been found in mutants or in filaments reconstituted in vitro. We analysed wild-type flagellin and flagellins from 17 flagellar-shape mutants (6 with straight filaments, 6 with curly filaments, 4 with coiled filaments and 1 with fl-type filament) by amino acid sequencing to identify the mutational sites. All mutant flagellins except that of the fl-type filament had single mutations; the fl-type flagellin had two mutations in the molecule. The sites of these mutations were localized in alpha-helical segments of the terminal regions of flagellin. A possible mechanism of the polymorphism of the flagellar filament is discussed.
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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
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pubmed:month |
Jun
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
219
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
471-80
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:2051483-Amino Acid Sequence,
pubmed-meshheading:2051483-Chromatography, High Pressure Liquid,
pubmed-meshheading:2051483-Cyanogen Bromide,
pubmed-meshheading:2051483-Flagella,
pubmed-meshheading:2051483-Flagellin,
pubmed-meshheading:2051483-Molecular Sequence Data,
pubmed-meshheading:2051483-Peptide Fragments,
pubmed-meshheading:2051483-Peptide Mapping,
pubmed-meshheading:2051483-Protein Conformation,
pubmed-meshheading:2051483-Salmonella typhimurium,
pubmed-meshheading:2051483-Trypsin
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pubmed:year |
1991
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pubmed:articleTitle |
Amino acids responsible for flagellar shape are distributed in terminal regions of flagellin.
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pubmed:affiliation |
ERATO, Research Development Corporation of Japan, Ibaraki.
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pubmed:publicationType |
Journal Article
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