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Structure paper

TitleStructural differences explain diverse functions of Plasmodium actins.
Journal, issue, pagesPLoS Pathog, Vol. 10, Issue 4, Page e1004091, Year 2014
Publish dateApr 17, 2014
AuthorsJuha Vahokoski / Saligram Prabhakar Bhargav / Ambroise Desfosses / Maria Andreadaki / Esa-Pekka Kumpula / Silvia Muñico Martinez / Alexander Ignatev / Simone Lepper / Friedrich Frischknecht / Inga Sidén-Kiamos / Carsten Sachse / Inari Kursula /
PubMed 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 ...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.
External linksPLoS Pathog / PubMed:24743229 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.3 - 25.0 Å
Structure data

EMDB-2572:
Cryo-EM structure of Plasmodium falciparum actin I
Method: EM (single particle) / Resolution: 25.0 Å

PDB-4cbu:
Crystal structure of Plasmodium falciparum actin I
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-4cbw:
Crystal structure of Plasmodium berghei actin I with D-loop from muscle actin
Method: X-RAY DIFFRACTION / Resolution: 2.501 Å

PDB-4cbx:
Crystal structure of Plasmodium berghei actin II
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE / 1,4-Dioxane

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-NA:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION / Phosphate

Source
  • plasmodium falciparum (malaria parasite P. falciparum)
  • mus musculus (house mouse)
  • plasmodium berghei (eukaryote)
  • synthetic construct (others)
KeywordsMOTOR PROTEIN / MALARIA / MOTILITY / PARASITE

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