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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dc.contributor.authorGarcía Linares, Sara
dc.contributor.authorMaula, Terhi
dc.contributor.authorRivera de la Torre, Esperanza
dc.contributor.authorGavilanes, José G.
dc.contributor.authorSlotte, J.Peter
dc.contributor.authorMartínez del Pozo, Álvaro
dc.date.accessioned2023-06-18T05:41:38Z
dc.date.available2023-06-18T05:41:38Z
dc.date.issued2016
dc.description.abstractActinoporins 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.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.departmentSección Deptal. de Bioquímica y Biología Molecular (Biológicas)
dc.description.facultyFac. de Ciencias Químicas
dc.description.facultyFac. de Ciencias Biológicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Ciencia e Innovación (MICINN)
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/40629
dc.identifier.doi10.1021/acs.biochem.6b00935
dc.identifier.issn0006-2960
dc.identifier.officialurlhttp://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00935
dc.identifier.urihttps://hdl.handle.net/20.500.14352/23063
dc.journal.titleBiochemistry
dc.language.isoeng
dc.page.final6420
dc.page.initial6406
dc.publisherAmerican Chemical Society
dc.relation.projectIDBFU2012-32404
dc.rights.accessRightsrestricted access
dc.subject.cdu577.1
dc.subject.keywordDriving forces
dc.subject.keywordHydrogen bonding properties
dc.subject.keywordHydrophobic effect
dc.subject.keywordMembrane binding
dc.subject.keywordPore forming toxins
dc.subject.keywordSpecific interaction
dc.subject.keywordSphingomyelin
dc.subject.keywordTryptophan residues
dc.subject.ucmBioquímica (Biología)
dc.subject.unesco2302 Bioquímica
dc.titleRole of the Tryptophan Residues in the Specific interaction of the Sea Anemone Stichodacty la helianthus’s Actinoporin Sticholysin II with Biological Membranes
dc.typejournal article
dc.volume.number55
dspace.entity.typePublication
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication.latestForDiscovery35824f7f-c79d-4928-9728-21124243bf7a
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