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Biochim Biophys Acta ; 1556(2-3): 142-8, 2002 Dec 02.
Article in English | MEDLINE | ID: mdl-12460671

ABSTRACT

ChaA, one of the sodium ion extrusion systems of Escherichia coli, was found to function at high pH [Biochim. Biophys. Acta 1363 (1998) 231]. A chaA-lacZ transcriptional fusion gene was constructed using chaA of E. coli O157:H7 and its expression was observed in strains derived from E. coli K12. The fusion gene was expressed at high pH and was induced by the addition of NaCl, KCl or sucrose. The amount of chaA mRNA measured by reverse transcription-polymerase chain reaction (RT-PCR) was increased by the addition of sucrose to alkaline growth medium. These results suggested that chaA expression was regulated by medium osmolarity and pH.


Subject(s)
Escherichia coli Proteins/metabolism , Escherichia coli/metabolism , Sodium/metabolism , Base Sequence , Biological Transport/physiology , Escherichia coli/genetics , Escherichia coli Proteins/genetics , Gene Expression Regulation, Bacterial , Genes, Reporter , Hydrogen-Ion Concentration , Molecular Sequence Data , Osmolar Concentration , Promoter Regions, Genetic , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sequence Alignment , Sucrose/metabolism
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