Linked Life Data

8617232

Source:http://linkedlifedata.com/resource/pubmed/id/8617232

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pubmed-article:8617232pubmed:abstractTextStaphylococcus aureus alpha-toxin is a hydrophilic polypeptide of 293 amino acids that produces heptameric transmembrane pores. During assembly, the formation of a pre-pore precedes membrane permeabilization; the latter is linked to a conformational change in the oligomer. Here, 41 single-cysteine replacement toxin mutants were thiol-specifically labelled with the polarity-sensitive fluorescent probe acrylodan. After oligomerization on membranes, only the mutants with acrylodan attached to residues in the sequence 118-140 exhibited a marked blue shift in the fluorescence emission maximum, indicative of movement of the fluorophore to a hydrophobic environment. Within this region, two functionally distinct parts could be identified. For mutants at positions 126-140, the shifts were partially reversed after membrane solubilization by detergents, indicating a direct interaction of the label with the membrane lipids. Membrane insertion of this sequence occurred together with the final pre-pore to pore transition of the heptamer. Thus residues 126-140 constitute a transmembrane sequence in the pore. With labelled residues 118-124, pre-pore assembly was the critical event to induce the spectral shifts, which persisted after the removal of membrane lipids and hence probably reflects protomer-protomer contacts within the heptamer. Finally, a derivative of the mutant N121C yielded occluded pores which could be opened by reductive reversal of the modification. Therefore this residue probably lines the lumen of the pore.lld:pubmed
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pubmed-article:8617232pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:8617232pubmed:year1996lld:pubmed
pubmed-article:8617232pubmed:articleTitleMolecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.lld:pubmed
pubmed-article:8617232pubmed:affiliationInstitute of Medical Microbiology and Hygiene, University of Mainz, Germany.lld:pubmed
pubmed-article:8617232pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8617232pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:8617232pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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