Interaction between the TolC and AcrA Proteins of a Multidrug Efflux System of Escherichia coli

AUTOR(ES)

Husain, Fasahath

FONTE

American Society for Microbiology

RESUMO

This paper provides the biochemical evidence for physical interactions between the outer membrane component, TolC, and the membrane fusion protein component, AcrA, of the major antibiotic efflux pump of Escherichia coli. Cross-linking between TolC and AcrA was independent of the presence of any externally added substrate of the efflux pump or of the pump protein, AcrB. The biochemical demonstration of a TolC-AcrA interaction is consistent with genetic studies in which extragenic suppressors of a mutant TolC strain were found in the acrA gene.

Documentos Relacionados

• Cross-Linked Complex between Oligomeric Periplasmic Lipoprotein AcrA and the Inner-Membrane-Associated Multidrug Efflux Pump AcrB from Escherichia coli
• Evidence that TolC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli.
• High-Level Fluoroquinolone-Resistant Clinical Isolates of Escherichia coli Overproduce Multidrug Efflux Protein AcrA
• High-Level Fluoroquinolone-Resistant Clinical Isolates of Escherichia coli Overproduce Multidrug Efflux Protein AcrA
• Chimeric Analysis of AcrA Function Reveals the Importance of Its C-Terminal Domain in Its Interaction with the AcrB Multidrug Efflux Pump