Structure and activity of the N-terminal region of the eukaryotic cytolysin equinatoxin II. (Articolo in rivista)

Type
Label
  • Structure and activity of the N-terminal region of the eukaryotic cytolysin equinatoxin II. (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/bi052166o (literal)
Alternative label
  • Drechsler A., Potrich C., Sabo J. K., Frisanco M., Guella G., Dalla Serra M., Anderluh G., Separovic F., Norton R. S. (2006)
    Structure and activity of the N-terminal region of the eukaryotic cytolysin equinatoxin II.
    in Biochemistry (Easton)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Drechsler A., Potrich C., Sabo J. K., Frisanco M., Guella G., Dalla Serra M., Anderluh G., Separovic F., Norton R. S. (literal)
Pagina inizio
  • 1818 (literal)
Pagina fine
  • 1828 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 45 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • The Walter & Eliza Hall Institute of Medical Research, 1G Royal Parade, ParkVille, Victoria 3050, Australia, School of Chemistry, UniVersity of Melbourne, Melbourne, Victoria 3010, Australia, ITC-CNR, Institute of Biophysics, Via SommariVe 18, 38050 PoVo (Trento), Italy Laboratory of Bioorganic Chemistry, Department of Physics, UniVersity of Trento, Via SommariVe 14, 38050 PoVo (Trento), Italy Department of Biology, Biotechnical Faculty, UniVersity of Ljubljana, Vecna pot 111, 1000 Ljubljana, SloVenia (literal)
Titolo
  • Structure and activity of the N-terminal region of the eukaryotic cytolysin equinatoxin II. (literal)
Abstract
  • The actinoporins are a family of proteins from sea anemones that lyse cells by forming pores in cell membranes. Sphingomyelin plays an important role in their lytic activity, with membranes lacking this lipid being resistant to these toxins. Pore formation by the actinoporin equinatoxin II (EqTII) proceeds by membrane binding via a surface rich in aromatic residues, followed by translocation of the N-terminal region to the membrane and, finally, across the bilayer to form a functional pore. A key feature of this mechanism is the ability of the N-terminal region to form a stable, bilayer-spanning helix in the membrane, which in turn requires dissociation of the N-terminus from the bulk of the protein and significant extension of the N-terminal helix of native EqTII. In this study the structures of three peptides corresponding to residues 11-29, 11-32, and 1-32, respectively, of EqTII have been investigated by high-resolution nuclear magnetic resonance and Fourier transform infrared spectroscopy. The 32-residue peptide lacks ordered secondary structure in water, but residues 6-28 form a helix in dodecylphosphocholine micelles. Although this helix is long enough to span a bilayer membrane, this peptide and the shorter analogues display limited permeabilizing activity in large unilamellar vesicles and very weak hemolytic activity in human red blood cells. Thus, while the N-terminal region has the structural features required for this unusual mechanism of pore formation, the lack of activity of the isolated N-terminus shows that the bulk of the protein is essential for efficient pore formation by facilitating initial membrane binding, interacting with sphingomyelin, or stabilizing the oligomeric pore. (literal)
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