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Evidence that the C‐terminus of OprM is involved in the assembly of the VceAB‐OprM efflux pump
Author(s) -
Bai Jiangping,
Mosley Lakysha,
Fralick Joe A.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.02.066
Subject(s) - efflux , chemistry , biophysics , microbiology and biotechnology , biology , biochemistry
Although the architecture of tripartite multiple drug resistance (MDR) efflux pumps of Gram‐negative bacteria has been well characterized, the means by which the components recognize each other and assemble into a functional pump remains obscure. In this study we present evidence that the C‐terminal domain of the Pseudomonas aeruginosa OprM and the α‐helical hairpin domain of Vibrio cholerae VceA play an important role in the recognition/specificity/recruitment step in the assembly of a functional, VceAB‐OprM chimeric efflux pump. To our knowledge, this is the first evidence directly linking the C‐terminal domain of an outer membrane efflux protein to its recruitment during the assembly of a tripartite efflux pump.