The topological localization of the subunit proteins of the three-component RND-efflux pump, MexAB-OprM in Pseudomonas aeruginossa

Taiji Nakae, Lan Guan, Hiroshi Yoneyama, Monika Germ, Akira Nakajima

研究成果: Article査読

抄録

The MexAB-OprM efflux pump of Pseudomonas aeruginosa consists of two inner and one outer membrane proteins and exports xenobiotics rendering the cells resistant to structurally diverse antimicrobial agents. We used fluorescent probes to monitor the pump function. Fluorescence intensity of hydrophobic cation, 2-(4-dimethylaminostyryl)-1-ethylpyridinium, was 7 to 4 times higher in the mutant lacking the pump subunit than the wild type strain. Water-soluble fluorescent probe, ethidium bromide, accumulated in the Mex mutants at the rate 5 times faster than in the wild-type cells. The results demonstrated that the fluorescent probes are powerful tools in real-time monitoring the function of the efffux pump. Topological of the MexB subunit showed that the protein span the membrane 12 times and had two huge periplasmic domains. MexA is an inner membrane anchoring lipoprotein and exposing entire polypeptide domain to the periplasmic space. OprM anchored the outer membrane via fatty acids and exposed the protein portion to the periplasmic space. These results suggested that the MexAB-OprM pump exports xenobiotics as that MexB drafts the substrates at the cytoplasmic membrane and export to periplasmic space and MexA and OprM convey the substrate bypassing the periplasmic space to the outer membrane.

本文言語English
ページ(範囲)106-117
ページ数12
ジャーナルProceedings of SPIE - The International Society for Optical Engineering
4625
DOI
出版ステータスPublished - 2002 1 1
外部発表はい

ASJC Scopus subject areas

  • 電子材料、光学材料、および磁性材料
  • 凝縮系物理学
  • コンピュータ サイエンスの応用
  • 応用数学
  • 電子工学および電気工学

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