An interbacterial NAD(P)<sup>+</sup> glycohydrolase toxin requires elongation factor Tu for delivery to target cells [electronic resource].
- Washington, D.C. : United States. Dept. of Energy. Office of Basic Energy Sciences, 2015.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
- Physical Description:
- pages 607-619 : digital, PDF file
- Additional Creators:
- Brookhaven National Laboratory
United States. Department of Energy. Office of Basic Energy Sciences
United States. Department of Energy. Office of Scientific and Technical Information
- Type VI secretion (T6S) influences the composition of microbial communities by catalyzing the delivery of toxins between adjacent bacterial cells. Here, we demonstrate that a T6S integral membrane toxin from <i>Pseudomonas aeruginosa</i>, Tse6, acts on target cells by degrading the universally essential dinucleotides NAD<sup>+</sup> and NADP<sup>+</sup>. Structural analyses of Tse6 show that it resembles mono-ADP-ribosyltransferase proteins, such as diphtheria toxin, with the exception of a unique loop that both excludes proteinaceous ADP-ribose acceptors and contributes to hydrolysis. We find that entry of Tse6 into target cells requires its binding to an essential housekeeping protein, translation elongation factor Tu (EF-Tu). These proteins participate in a larger assembly that additionally directs toxin export and provides chaperone activity. Lastly, visualization of this complex by electron microscopy defines the architecture of a toxin-loaded T6S apparatus and provides mechanistic insight into intercellular membrane protein delivery between bacteria.
- Published through SciTech Connect.
Cell 163 3 ISSN 0092-8674 AM
John C. Whitney; Dennis Quentin; Shin Sawai; Michele LeRoux; Brittany N. Harding; Hannah E. Ledvina; Bao Q. Tran; Howard Robinson; Young Ah Goo; David R. Goodlett; Stefan Raunser; Joseph D. Mougous.
- Funding Information:
View MARC record | catkey: 24056738