Journal
JOURNAL OF BACTERIOLOGY
Volume 192, Issue 17, Pages 4498-4503Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00334-10
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Funding
- National Research Foundation of Korea [NRF-2009-0072268]
- Ministry of Education, Science and Technology, Republic of Korea [20100002201]
- 21C Frontier Microbial Genomics and Application Center Program
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Tripartite efflux pumps found in Gram-negative bacteria are involved in antibiotic resistance and toxicprotein secretion. In this study, we show, using site-directed mutational analyses, that the conserved residues located in the tip region of the alpha-hairpin of the membrane fusion protein (MFP) AcrA play an essential role in the action of the tripartite efflux pump AcrAB-TolC. In addition, we provide in vivo functional data showing that both the length and the amino acid sequence of the alpha-hairpin of AcrA can be flexible for the formation of a functional AcrAB-TolC pump. Genetic-complementation experiments further indicated functional interrelationships between the AcrA hairpin tip region and the TolC aperture tip region. Our findings may offer a molecular basis for understanding the multidrug resistance of pathogenic bacteria.
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