The alpha-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-TolCopen access
- Authors
- Lee, Minho; Kim, Hyun-Lee; Song, Saemee; Joo, Minju; Lee, Seunghwa; Kim, Daeyoung; Hahn, Yoonsoo; Ha, Nam-Chul; Lee, Kangseok
- Issue Date
- Apr-2013
- Publisher
- MICROBIOLOGICAL SOCIETY KOREA
- Keywords
- MacA; MacB; TolC; TolCV1; TolCV2; Type I secretion system
- Citation
- JOURNAL OF MICROBIOLOGY, v.51, no.2, pp 154 - 159
- Pages
- 6
- Journal Title
- JOURNAL OF MICROBIOLOGY
- Volume
- 51
- Number
- 2
- Start Page
- 154
- End Page
- 159
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/14747
- DOI
- 10.1007/s12275-013-2699-3
- ISSN
- 1225-8873
1976-3794
- 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 alpha-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 Gram-negative bacteria.
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