REAL

Functional truncated membrane pores

Stoddart, David and Ayub, Mariam and Höfler, Lajos and Raychaudhuri, Pinky and Klingelhoefer, Jochen W. and Maglia, Giovanni and Heron, Andrew and Bayley, Hagan (2014) Functional truncated membrane pores. Proceedings of the National Academy of Sciences of the United States of America, 111 (7). pp. 2425-2430. ISSN 1091-6490

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Abstract

Membrane proteins are generally divided into two classes. Integral proteins span the lipid bilayer, and peripheral proteins are located at the membrane surface. Here, we provide evidence for membrane proteins of a third class that stabilize lipid pores, most probably as toroidal structures. We examined mutants of the staphylococcal a-hemolysin pore so severely truncated that the protein cannot span a bilayer. Nonetheless, the doughnut-like structures elicited well-defined transmembrane ionic currents by inducing pore formation in the underlying lipids. The formation of lipid pores, produced here by a structurally defined protein, is supported by the lipid and voltage dependences of pore formation, and by molecular dynamics simulations. We discuss the role of stabilized lipid pores in amyloid disease, the action of antimicrobial peptides, and the assembly of the membrane-attack complexes of the immune system.

Item Type: Article
Additional Information: cited By (since 1996)2
Uncontrolled Keywords: alpha-hemolysin; beta-barrel; lipid reorganization; nanopore, Bacterial Toxins; Cell Membrane Permeability; Hemolysin Proteins; Lipid Bilayers; Membrane Proteins; Models, Molecular; Molecular Dynamics Simulation; Mutagenesis; Polymerase Chain Reaction; Protein Conformation
Subjects: Q Science / természettudomány > QD Chemistry / kémia > QD02 Physical chemistry / fizikai kémia
Depositing User: Dr Lajos Höfler
Date Deposited: 17 Sep 2014 09:15
Last Modified: 17 Sep 2014 09:15
URI: http://real.mtak.hu/id/eprint/14506

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