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dc.contributor.authorVahokoski, Juha
dc.contributor.authorBhargav, Saligram Prabhakar
dc.contributor.authorDesfosses, Ambroise
dc.contributor.authorAndreadaki, Maria
dc.contributor.authorKumpula, Esa-Pekka
dc.contributor.authorMartinez, Silvia Muñico
dc.contributor.authorIgnatev, Alexander
dc.contributor.authorLepper, Simone
dc.contributor.authorFrischknecht, Friedrich
dc.contributor.authorSidén-Kiamos, Inga
dc.contributor.authorSachse, Carsten
dc.contributor.authorKursula, Inari
dc.date.accessioned2014-04-22T12:36:37Zen
dc.date.available2014-04-22T12:36:37Zen
dc.date.issued2014-04en
dc.identifier.citationStructural differences explain diverse functions of Plasmodium actins. 2014, 10 (4):e1004091 PLoS Pathog.en
dc.identifier.issn1553-7374en
dc.identifier.pmid24743229en
dc.identifier.doi10.1371/journal.ppat.1004091en
dc.identifier.urihttp://hdl.handle.net/10033/316036en
dc.description.abstractActins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than α-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.
dc.language.isoenen
dc.rightsArchived with thanks to PLoS pathogensen
dc.titleStructural differences explain diverse functions of Plasmodium actins.en
dc.typeArticleen
dc.contributor.departmentStrucural biology of the cytoskeleton, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.en
dc.identifier.journalPLoS pathogensen
refterms.dateFOA2018-06-12T23:16:51Z
html.description.abstractActins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than α-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.


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