Linked Life Data

10411266

Source:http://linkedlifedata.com/resource/pubmed/id/10411266

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-8-30
pubmed:databankReference
pubmed:abstractText
The fliA gene encodes the flagellum-specific sigma factor sigma28 In Salmonella typhimurium. The transcription in vivo and in vitro of this gene was analysed and it was found that there are two promoters for the expression of this gene. One is a class 2 promoter which is recognized by sigma70-RNA polymerase in the presence of the FlhD and FlhC activator proteins. The other is a class 3 promoter which is recognized by sigma28-RNA polymerase. Therefore, the fliA operon is under dual positive control from FlhD/FlhC and from FliA itself. The nucleotide sequence downstream of the fliA gene was determined. The sequence contains two ORFs following the fliA gene. On the basis of their sequence homology, it is concluded that these two correspond to the fliZ and fliY genes of Escherichia coil. Northern blot analysis revealed that the fliZ gene is transcribed from the fliA promoters, whereas the fliY gene is transcribed from both the fliA promoters and its own FlhD/FlhC-independent promoter. A fliZ-disruption mutant was constructed by inserting a kanamycin-resistance gene cassette into the fliZ gene on the chromosome. The mutant showed poor motility, and introduction of a fliZ+ plasmid into this mutant restored the wildtype level of motility. These results suggest that the fliZ gene may be required for expression of maximal motility.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
145 ( Pt 6)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1389-96
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Structure and expression of the fliA operon of Salmonella typhimurium.
pubmed:affiliation
Department of Applied Biochemistry, Faculty of Applied Biological Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't