Deletion of the Escherichia coli uup gene encoding a protein of the ATP binding cassette superfamily affects bacterial competitiveness.
Bacteria use a variety of mechanisms for intercellular communication. Here we show that deletion of the uup gene, which encodes a soluble ATP binding cassette (ABC) ATPase, renders the mutant strain sensitive to its parent when they are grown together in the same medium. Our data suggest that the decrease in viability of the mutant is dependent on direct cell-to-cell contact with the parent strain. Furthermore, we show that the presence of intact Walker B motifs in Uup is required for immunity or resistance to the parental strain, suggesting that ATP hydrolysis is an important determinant of this phenotype.
Unité des Membranes Bactériennes CNRS URA2172, Département de Microbiologie, Institut Pasteur 25, Rue du Docteur Roux, 75724 Paris Cedex 15, France.
Dorothée
D
Murat
Laurent
L
Goncalves
Elie
E
Dassa
D018528:ATP-Binding Cassette Transporters / Q000235:genetics* / Q000502:physiology; D000251:Adenosine Triphosphatases / Q000235:genetics / Q000502:physiology; D000255:Adenosine Triphosphate / Q000378:metabolism; D002450:Cell Communication; D015169:Colony Count, Microbial; D003470:Culture Media; D004251:DNA Transposable Elements; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development* / Q000502:physiology; D029968:Escherichia coli Proteins / Q000235:genetics*; D017353:Gene Deletion; D006868:Hydrolysis
D018528:ATP-Binding Cassette Transporters; D003470:Culture Media; D004251:DNA Transposable Elements; D029968:Escherichia coli Proteins; C105795:Uup protein, E coli; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases