Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.

ABSTRACT: Crystallographic data of the dimeric and octameric forms of fragaceatoxin C (FraC) suggested the key role of a small hydrophobic protein-protein interaction surface for actinoporins oligomerization and pore formation in membranes. However, site-directed mutagenesis studies supporting this hypothesis for others actinoporins are still lacking. Here, we demonstrate that disrupting the key hydrophobic interaction between V60 and F163 (FraC numbering scheme) in the oligomerization interface of FraC, equinatoxin II (EqtII), and sticholysin II (StII) impairs the pore formation activity of these proteins. Our results allow for the extension of the importance of FraC protein-protein interactions in the stabilization of the oligomeric intermediates of StII and EqtII pointing out that all of these pr

SUBMITTER: Mesa-Galloso H 

PROVIDER: S-EPMC5326555 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature