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A Novel Dynamin-Related Protein Has Been Recruited for Apicoplast Fission in Toxoplasma gondii

van Dooren, Giel; Reiff, Sarah B.; Tomova, Cveta; Meissner, Markus; Humbel, Bruno M.; Striepen, Boris

Description

Background: Apicomplexan parasites cause numerous important human diseases, including malaria and toxoplasmosis. Apicomplexa belong to the Alveolata, a group that also includes ciliates and dinoflagellates. Apicomplexa retain a plastid organelle (the apicoplast) that was derived from an endosymbiotic relationship between the alveolate ancestor and a red alga. Apicoplasts are essential for parasite growth and must correctly divide and segregate into daughter cells upon cytokinesis. Apicoplast...[Show more]

dc.contributor.authorvan Dooren, Giel
dc.contributor.authorReiff, Sarah B.
dc.contributor.authorTomova, Cveta
dc.contributor.authorMeissner, Markus
dc.contributor.authorHumbel, Bruno M.
dc.contributor.authorStriepen, Boris
dc.date.accessioned2015-12-13T22:45:26Z
dc.identifier.issn0960-9822
dc.identifier.urihttp://hdl.handle.net/1885/79782
dc.description.abstractBackground: Apicomplexan parasites cause numerous important human diseases, including malaria and toxoplasmosis. Apicomplexa belong to the Alveolata, a group that also includes ciliates and dinoflagellates. Apicomplexa retain a plastid organelle (the apicoplast) that was derived from an endosymbiotic relationship between the alveolate ancestor and a red alga. Apicoplasts are essential for parasite growth and must correctly divide and segregate into daughter cells upon cytokinesis. Apicoplast division depends on association with the mitotic spindle, although little is known about the molecular machinery involved in this process. Apicoplasts lack the conserved machinery that divides chloroplasts in plants and red algae, suggesting that these mechanisms are unique. Results: Here, we demonstrate that a dynamin-related protein in Toxoplasma gondii (TgDrpA) localizes to punctate regions on the apicoplast surface. We generate a conditional dominant-negative TgDrpA cell line to disrupt TgDrpA functions and demonstrate that TgDrpA is essential for parasite growth and apicoplast biogenesis. Fluorescence recovery after photobleaching and time-lapse imaging studies provide evidence for a direct role for TgDrpA in apicoplast fission. Conclusions: Our data suggest that DrpA was likely recruited from the alveolate ancestor to function in fission of the symbiont and ultimately replaced the conserved division machinery of that symbiont.
dc.publisherCell Press
dc.sourceCurrent Biology
dc.subjectKeywords: dynamin; hybrid protein; microtubule associated protein; protozoal protein; animal; article; cell culture; cell organelle; classification; cytology; fibroblast; genetics; human; metabolism; phylogeny; Toxoplasma; ultrastructure; Animals; Cells, Cultured; CELLBIO; EVO_ECOL
dc.titleA Novel Dynamin-Related Protein Has Been Recruited for Apicoplast Fission in Toxoplasma gondii
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume19
dc.date.issued2009
local.identifier.absfor060104 - Cell Metabolism
local.identifier.ariespublicationf5625xPUB8159
local.type.statusPublished Version
local.contributor.affiliationvan Dooren, Giel, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationReiff, Sarah B., University of Georgia
local.contributor.affiliationTomova, Cveta, Utrecht University
local.contributor.affiliationMeissner, Markus, Heidelberg University School of Medicine
local.contributor.affiliationHumbel, Bruno M., Utrecht University
local.contributor.affiliationStriepen, Boris, University of Georgia
local.description.embargo2037-12-31
local.bibliographicCitation.issue4
local.bibliographicCitation.startpage267
local.bibliographicCitation.lastpage276
local.identifier.doi10.1016/j.cub.2008.12.048
local.identifier.absseo920109 - Infectious Diseases
dc.date.updated2016-02-24T09:39:59Z
local.identifier.scopusID2-s2.0-60349117040
local.identifier.thomsonID000263779600018
CollectionsANU Research Publications

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