A yeast toxic mutant of HET-s amyloid disrupts membrane integrity

Biochimica Et Biophysica Acta
Ha Phuong TaSophie Lecomte

Abstract

Many studies have pointed out the interaction between amyloids and membranes, and their potential involvement in amyloid toxicity. Previously, we generated a yeast toxic amyloid mutant (M8) from the harmless amyloid protein by changing a few residues of the Prion Forming Domain of HET-s (PFD HET-s(218-289)) and clearly demonstrated the complete different behaviors of the non-toxic Wild Type (WT) and toxic amyloid (called M8) in terms of fiber morphology, aggregation kinetics and secondary structure. In this study, we compared the interaction of both proteins (WT and M8) with membrane models, as liposomes or supported bilayers. We first demonstrated that the toxic protein (M8) induces a significant leakage of liposomes formed with negatively charged lipids and promotes the formation of microdomains inside the lipid bilayer (as potential "amyloid raft"), whereas the non-toxic amyloid (WT) only binds to the membrane without further perturbations. The secondary structure of both amyloids interacting with membrane is preserved, but the anti-symmetric PO(2)(-) vibration is strongly shifted in the presence of M8. Secondly, we established that the presence of membrane models catalyzes the amyloidogenesis of both proteins. Cryo-TEM (cry...Continue Reading

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Citations

Apr 22, 2014·Biochimica Et Biophysica Acta·Sarah ElaidSerge Bouaziz
Sep 17, 2013·Biochimica Et Biophysica Acta·Karine BerthelotFrédéric Peruch
Mar 27, 2018·Biological Reviews of the Cambridge Philosophical Society·Douglas B Kell, Etheresia Pretorius

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