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Role of the Tryptophan Residues in the Specific interaction of the Sea Anemone Stichodacty la helianthus’s Actinoporin Sticholysin II with Biological Membranes

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García Linares, Sara and Maula, Terhi and Rivera de la Torre, Esperanza and Gavilanes, José G. and Slotte, J.Peter and Martínez del Pozo, Álvaro (2016) Role of the Tryptophan Residues in the Specific interaction of the Sea Anemone Stichodacty la helianthus’s Actinoporin Sticholysin II with Biological Membranes. Biochemistry, 55 . pp. 6406-6420. ISSN 0006-2960

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Official URL: http://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00935



Abstract

Actinoporins are pore-forming toxins from sea anemones. Upon interaction with sphingomyelin-containing bilayers, they become integral oligomeric membrane structures that form a pore. Sticholysin II from Stichodactyla helianthus contains five tryptophans located at strategic positions; its role has now been studied using different mutants. Results show that W43 and W115 play a eterminant role in maintaining the high thermostability of the protein, while W146 provides specific interactions for protomer−protomer assembly. W110 and W114 sustain the hydrophobic effect, which is one of the major driving forces for membrane binding in the presence of Chol. However, in its absence, additional interactions with sphingomyelin are required. These conclusions were confirmed with two sphingomyelin analogues, one of which had impaired hydrogen bonding properties. The results obtained support actinoporins’ Trp residues playing a major role in membrane recognition and binding, but their residues have an only minor influence on the diffusion and oligomerization steps needed to assemble a functional pore.


Item Type:Article
Uncontrolled Keywords:Driving forces; Hydrogen bonding properties; Hydrophobic effect; Membrane binding; Pore forming toxins; Specific interaction; Sphingomyelin; Tryptophan residues
Subjects:Medical sciences > Biology > Biochemistry
ID Code:40629
Deposited On:21 Dec 2016 09:40
Last Modified:09 Jun 2017 08:09

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