2.50
Hdl Handle:
http://hdl.handle.net/10033/316036
Title:
Structural differences explain diverse functions of Plasmodium actins.
Authors:
Vahokoski, Juha; Bhargav, Saligram Prabhakar; Desfosses, Ambroise; Andreadaki, Maria; Kumpula, Esa-Pekka; Martinez, Silvia Muñico; Ignatev, Alexander; Lepper, Simone; Frischknecht, Friedrich; Sidén-Kiamos, Inga; Sachse, Carsten; Kursula, Inari ( 0000-0001-5236-7056 )
Abstract:
Actins 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.
Affiliation:
Strucural biology of the cytoskeleton, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.
Citation:
Structural differences explain diverse functions of Plasmodium actins. 2014, 10 (4):e1004091 PLoS Pathog.
Journal:
PLoS pathogens
Issue Date:
Apr-2014
URI:
http://hdl.handle.net/10033/316036
DOI:
10.1371/journal.ppat.1004091
PubMed ID:
24743229
Type:
Article
Language:
en
ISSN:
1553-7374
Appears in Collections:
publications of the research group CSSB

Full metadata record

DC FieldValue Language
dc.contributor.authorVahokoski, Juhaen
dc.contributor.authorBhargav, Saligram Prabhakaren
dc.contributor.authorDesfosses, Ambroiseen
dc.contributor.authorAndreadaki, Mariaen
dc.contributor.authorKumpula, Esa-Pekkaen
dc.contributor.authorMartinez, Silvia Muñicoen
dc.contributor.authorIgnatev, Alexanderen
dc.contributor.authorLepper, Simoneen
dc.contributor.authorFrischknecht, Friedrichen
dc.contributor.authorSidén-Kiamos, Ingaen
dc.contributor.authorSachse, Carstenen
dc.contributor.authorKursula, Inarien
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.en
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

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