Precise excision and secondary transposition of TnphoA in non-motile mutants of a Salmonella enterica serovar Enteritidis clinical isolate

Abstract Mutagenesis with TnphoA has been widely used in many bacteria. Here, we report the excision and secondary transposition of this transposon in three non-motile (fliC, fliF and motB) mutants of Salmonella enterica serovar Enteritidis (S. Enteritidis). Isolation of motile revertants showed tha...

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Bibliographic Details
Published in:FEMS microbiology letters 2005-04, Vol.245 (2), p.263-269
Main Authors: Amy, Maı?té, Virlogeux-Payant, Isabelle, Bottreau, Elisabeth, Mompart, Florence, Pardon, Pierre, Velge, Philippe
Format: Article
Language:English
Subjects:
Alkaline Phosphatase
Bacterial Proteins - genetics
Bacterial Proteins - physiology
Bacteriology
Biological and medical sciences
Cyclin-Dependent Kinases - genetics
Cyclin-Dependent Kinases - metabolism
DNA Transposable Elements
Flagella
Flagella - physiology
Flagella - ultrastructure
Flagellin - genetics
Fundamental and applied biological sciences. Psychology
Genetics
Genomes
Kanamycin
Life Sciences
Membrane Proteins - genetics
Membrane Proteins - physiology
Microbiology
Microbiology and Parasitology
Movement
Mutagenesis
Mutants
Mutation
Recombination, Genetic
Revertants
Salmonella
Salmonella enterica
Salmonella Enteritidis
Salmonella enteritidis - genetics
Salmonella enteritidis - physiology
Transposase
Transposase gene
Transposition
Transposons
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Summary:Abstract Mutagenesis with TnphoA has been widely used in many bacteria. Here, we report the excision and secondary transposition of this transposon in three non-motile (fliC, fliF and motB) mutants of Salmonella enterica serovar Enteritidis (S. Enteritidis). Isolation of motile revertants showed that they were kanamycin resistant and conserved a copy of TnphoA in their genome in an insertion site different from the initial one. They also expressed an intact flagella. Characterization of the motile revertant derived from the fliC mutant showed that TnphoA excised precisely from the fliC gene, resulting in an equivalent amount of FliC secreted protein in the revertant compared to that of the wild-type strain. These results show that TnphoA mutants should be used with care and underline the value of using transposon derivatives lacking the transposase gene.
ISSN:0378-1097
1574-6968
DOI:10.1016/j.femsle.2005.03.018