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Article Dans Une Revue Cellular and Molecular Life Sciences Année : 2008

A molecular pin to study the dynamics of β-barrel formation in pore-forming toxins on erythrocytes: a sliding model

Olivier Joubert
G. Viero
  • Fonction : Auteur
A. Gropuzzo
  • Fonction : Auteur
D. Keller
G. Prévost
  • Fonction : Auteur
M. Dalla Serra
  • Fonction : Auteur

Résumé

gamma-Hemolysins are pore-forming toxins which develop from water-soluble monomers by combining two different 'albeit homologous' proteins. They form oligomeric pores in both cell and model membranes by undergoing a still poorly understood conformational rearrangement in the stem region. The stem is formed by three beta-strands, folded onto the core of the soluble protein and completely extended in the pore. We propose a new model to explain such a process. Seven double-cysteine mutants were developed by inserting one cysteine on the stretch that links the beta-hairpin to the core of the protein and another on different positions along the beta-strands. The membrane bound protein was blocked in a non-lytic state by S-S bond formation. Six mutants were oxidized as inactive intermediates, but became active after adding DTT. These results demonstrate that the stem extension can be temporarily frozen and that the beta-barrel formation occurs by beta-strand concerted step-by-step sliding.

Dates et versions

hal-03449981 , version 1 (25-11-2021)

Identifiants

Citer

Olivier Joubert, G. Viero, A. Gropuzzo, D. Keller, G. Prévost, et al.. A molecular pin to study the dynamics of β-barrel formation in pore-forming toxins on erythrocytes: a sliding model. Cellular and Molecular Life Sciences, 2008, 65 (2), pp.312-323. ⟨10.1007/s00018-007-7491-2⟩. ⟨hal-03449981⟩
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