OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity

FEBS Letters

Walker, Daniel C³  Law, Christopher J³  Penfold, Christopher N¹  Moore, Geoffrey R²  James, Richard¹  Kleanthous, Colin³ 

[1] Division of Microbiology and Infectious Diseases, Queens Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK;School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich NR4 7TJ, UK;Department of Biology, University of York, York YO10 5YW, UK

关键词: BtuB;    OmpF;    Porin;    Bacteriocin;    Colicin translocation;    Protein–protein interaction;    OM;    outer membrane;    LIS;    lithium diiodosalicylate;    OG;    n-octyl-β-D-glucopyranoside;    LPS;    lipopolysaccharide;    Free colicin E9;    colicin from which its immunity protein Im9 has been removed;    Colicin E9 T-R;    truncated colicin in which the C-terminal endonuclease domain has been deleted;   

DOI  :  10.1016/S0014-5793(03)00511-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The outer membrane (OM) vitamin B₁₂ receptor, BtuB, is the primary receptor for E group colicin adsorption to Escherichia coli. Cell death by this family of toxins requires the OM porin OmpF but its role remains elusive. We show that OmpF enhances the ability of purified BtuB to protect bacteria against the endonuclease colicin E9, demonstrating either that the two OM proteins form the functional receptor or that OmpF is recruited for subsequent translocation of the bacteriocin. While stable binary colicin E9–BtuB complexes could be readily shown in vitro, OmpF-containing complexes could not be detected, implying that OmpF association with the BtuB–colicin complex, while necessary, must be weak and/or transient in nature.

【 授权许可】

Unknown