|
KMID : 0880220130510020154
|
|
Journal of Microbiology
2013 Volume.51 No. 2 p.154 ~ p.159
|
|
|
The α-barrel tip region of Escherichia coli TolC homologs of Vibrio vulnificus interacts with the MacA protein to form the functional macrolide-specific efflux pump MacAB-TolC
|
|
Lee Min-Ho
Kim Hyun-Lee
Song Sae-Mee
Joo Min-Ju
Lee Seung-Hwa
Kim Dae-Young
Hahn Yoon-Soo
Lee Kang-Seok
Ha Nam-Chul
|
|
|
Abstract
|
|
|
|
TolC and its homologous family of proteins are outer membrane factors that are essential for exporting small molecules and toxins across the outer membrane in Gram-negative bacteria. Two open reading frames in the Vibrio vulnificus genome that encode proteins homologous to Escherichia coli TolC, designated TolCV1 and TolCV2, have 51.3% and 29.6% amino acid identity to TolC, respectively. In this study, we show that TolCV1 and TolCV2 functionally and physically interacted with the membrane fusion protein, MacA, a component of the macrolide-specific MacAB-TolC pump of E. coli. We further show that the conserved residues located at the aperture tip region of the α-hairpin of TolCV1 and TolCV2 played an essential role in the formation of the functional MacAB-TolC pump using site-directed mutational analyses. Our findings suggest that these outer membrane factors have conserved tip-to-tip interaction with the MacA membrane fusion protein for action of the drug efflux pump in Gramnegative bacteria.
|
|
|
KEYWORD
|
|
|
MacA, MacB, TolC, TolCV1, TolCV2, Type I secretion system
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|