Structural differences explain diverse functions of Plasmodium actins.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Bhargav, Saligram Prabhakar
Martinez, Silvia Muñico
MetadataShow full item record
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.
CitationStructural differences explain diverse functions of Plasmodium actins. 2014, 10 (4):e1004091 PLoS Pathog.
AffiliationStrucural biology of the cytoskeleton, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.
The following license files are associated with this item:
- Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.
- Authors: Singh BK, Sattler JM, Chatterjee M, Huttu J, Schüler H, Kursula I
- Issue date: 2011 Aug 12
- Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability.
- Authors: Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I, Raunser S
- Issue date: 2017 Oct 3
- A mechanism for actin filament severing by malaria parasite actin depolymerizing factor 1 via a low affinity binding interface.
- Authors: Wong W, Webb AI, Olshina MA, Infusini G, Tan YH, Hanssen E, Catimel B, Suarez C, Condron M, Angrisano F, Nebi T, Kovar DR, Baum J
- Issue date: 2014 Feb 14
- Minimal requirements for actin filament disassembly revealed by structural analysis of malaria parasite actin-depolymerizing factor 1.
- Authors: Wong W, Skau CT, Marapana DS, Hanssen E, Taylor NL, Riglar DT, Zuccala ES, Angrisano F, Lewis H, Catimel B, Clarke OB, Kershaw NJ, Perugini MA, Kovar DR, Gulbis JM, Baum J
- Issue date: 2011 Jun 14
- Pivotal and distinct role for Plasmodium actin capping protein alpha during blood infection of the malaria parasite.
- Authors: Ganter M, Rizopoulos Z, Schüler H, Matuschewski K
- Issue date: 2015 Apr