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Biochemical and biophysical research communications v.494 no.3/4, 2017년, pp.668 - 673   SCI SCIE
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Stoichiometry and mechanistic implications of the MacAB-TolC tripartite efflux pump

Jo, Inseong (Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea ) ; Hong, Seokho (Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea ) ; Lee, Minho (Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea ) ; Song, Saemee (Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea ) ; Kim, Jin-Sik (Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea ) ; Mitra, Alok K. (School of Biological Sciences, The University of Auckland, Auckland 1010, New Zealand ) ; Hyun, Jaekyung (Electron Microscopy Research Center, Korea Basic Scie ) ; Lee, Kangseok ; Ha, Nam-Chul ;
  • 초록  

    Abstract The MacAB-TolC tripartite efflux pump is involved in resistance to macrolide antibiotics and secretion of protein toxins in many Gram-negative bacteria. The pump spans the entire cell envelope and operates by expelling substances to extracellular space. X-ray crystal and electron microscopic structures have revealed the funnel-like MacA hexamer in the periplasmic space and the cylindrical TolC trimer. Nonetheless, the inner membrane transporter MacB still remains ambiguous in terms of its oligomeric state in the functional complex. In this study, we purified a stable binary complex using a fusion protein of MacA and MacB of Escherichia coli , and then supplemented MacA to meet the correct stoichiometry between the two proteins. The result demonstrated that MacB is a homodimer in the complex, which is consistent with results from the recent complex structure using cryo-electron microscopy single particle analysis. Structural comparison with the previously reported MacB periplasmic domain structure suggests a molecular mechanism for regulation of the activity of MacB via an interaction between the MacB periplasmic domain and MacA. Our results provide a better understanding of the tripartite pumps at the molecular level. Highlights The exact stoichiometry of the MacAB-TolC pump was confirmed. Structural comparison provides a mechanism for MacA-dependent MacB activation. Improving understanding of the regulatory mechanisms of other efflux pumps.


  • 주제어

    Escherichia coli .   Actinobacillus actinomycetemcomitans .   Tripartite efflux pump .   MacAB-TolC .   Electron microscopy.  

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