Structural differences explain diverse functions of Plasmodium actins.

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 obse...

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Autores principales:	Juha 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
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c5325fd5c9e44a88a184c7df2fc0ead6
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spelling	oai:doaj.org-article:c5325fd5c9e44a88a184c7df2fc0ead62021-11-18T06:06:42ZStructural differences explain diverse functions of Plasmodium actins.1553-73661553-737410.1371/journal.ppat.1004091https://doaj.org/article/c5325fd5c9e44a88a184c7df2fc0ead62014-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24743229/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Actins 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.Juha VahokoskiSaligram Prabhakar BhargavAmbroise DesfossesMaria AndreadakiEsa-Pekka KumpulaSilvia Muñico MartinezAlexander IgnatevSimone LepperFriedrich FrischknechtInga Sidén-KiamosCarsten SachseInari KursulaPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 10, Iss 4, p e1004091 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Juha 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 Structural differences explain diverse functions of Plasmodium actins.
description	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.
format	article
author	Juha 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
author_facet	Juha 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
author_sort	Juha Vahokoski
title	Structural differences explain diverse functions of Plasmodium actins.
title_short	Structural differences explain diverse functions of Plasmodium actins.
title_full	Structural differences explain diverse functions of Plasmodium actins.
title_fullStr	Structural differences explain diverse functions of Plasmodium actins.
title_full_unstemmed	Structural differences explain diverse functions of Plasmodium actins.
title_sort	structural differences explain diverse functions of plasmodium actins.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/c5325fd5c9e44a88a184c7df2fc0ead6
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Structural differences explain diverse functions of Plasmodium actins.

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