A novel mechanism of pore-formation: quinatoxin penetration of membrane by a N-terminal amphipatic region. (Articolo in rivista)

Type
Label
  • A novel mechanism of pore-formation: quinatoxin penetration of membrane by a N-terminal amphipatic region. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Malovrh P. 1, Viero G. 2, Dalla Serra M. 2, Podlesek Z. 1, Lakey J. H. 3, Macek P. 1, Menestrina G. 2, Anderluh G. 1 (2003)
    A novel mechanism of pore-formation: quinatoxin penetration of membrane by a N-terminal amphipatic region.
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Malovrh P. 1, Viero G. 2, Dalla Serra M. 2, Podlesek Z. 1, Lakey J. H. 3, Macek P. 1, Menestrina G. 2, Anderluh G. 1 (literal)
Pagina inizio
  • 22678 (literal)
Pagina fine
  • 22685 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 278 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1: Uni Ljubljana; 2: CNR; 3: Uni Newcastle upon Tyne, UK (literal)
Titolo
  • A novel mechanism of pore-formation: quinatoxin penetration of membrane by a N-terminal amphipatic region. (literal)
Abstract
  • Equinatoxin II is a representative of actinoporins, eukaryotic pore-forming toxins from sea anemones. It creates pores in natural and artificial lipid membranes by an association of three or four monomers. Cysteine-scanning mutagenesis was used to study the structure of the N terminus, which is proposed to be crucial in transmembrane pore formation. We provide data for two steps of pore formation: a lipid-bound monomeric intermediate state and a final oligomeric pore. Results show that residues 10-28 are organized as an alpha-helix in both steps. In the first step, the whole region is transferred to a lipid-water interface, laying flat on the membrane. In the pore-forming state, the hydrophilic side of the amphipathic helix lines the pore lumen. The pore has a restriction around Asp-10, according to the permeabilization ratio of ions flowing through pores formed by chemically modified mutants. A general model was introduced to derive the tilt angle of the helix from the ion current data. This study reveals that actinoporins use a unique single helix insertion mechanism for pore formation. (literal)
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