2.50
Hdl Handle:
http://hdl.handle.net/10033/603604
Title:
The lasso segment is required for functional dimerization of the Plasmodium formin 1 FH2 domain.
Authors:
Ignatev, Alexander; Bhargav, Saligram Prabhakar; Vahokoski, Juha; Kursula, Petri ( 0000-0001-8529-3751 ) ; Kursula, Inari ( 0000-0001-5236-7056 )
Abstract:
Apicomplexan parasites, such as the malaria-causing Plasmodium species, utilize a unique way of locomotion and host cell invasion. This substrate-dependent gliding motility requires rapid cycling of actin between the monomeric state and very short, unbranched filaments. Despite the crucial role of actin polymerization for the survival of the malaria parasite, the majority of Plasmodium cellular actin is present in the monomeric form. Plasmodium lacks most of the canonical actin nucleators, and formins are essentially the only candidates for this function in all Apicomplexa. The malaria parasite has two formins, containing conserved formin homology (FH) 2 and rudimentary FH1 domains. Here, we show that Plasmodium falciparum formin 1 associates with and nucleates both mammalian and Plasmodium actin filaments. Although Plasmodium profilin alone sequesters actin monomers, thus inhibiting polymerization, its monomer-sequestering activity does not compete with the nucleating activity of formin 1 at an equimolar profilin-actin ratio. We have determined solution structures of P. falciparum formin 1 FH2 domain both in the presence and absence of the lasso segment and the FH1 domain, and show that the lasso is required for the assembly of functional dimers.
Affiliation:
Helmholtz Centre for Infection Research, University of Hamburg, and German Electron Synchrotron (DESY), Hamburg, Germany.
Citation:
The lasso segment is required for functional dimerization of the Plasmodium formin 1 FH2 domain. 2012, 7 (3):e33586 PLoS ONE
Journal:
PloS one
Issue Date:
2012
URI:
http://hdl.handle.net/10033/603604
DOI:
10.1371/journal.pone.0033586
PubMed ID:
22428073
Type:
Article
Language:
en
ISSN:
1932-6203
Appears in Collections:
publications of the research group CSSB

Full metadata record

DC FieldValue Language
dc.contributor.authorIgnatev, Alexanderen
dc.contributor.authorBhargav, Saligram Prabhakaren
dc.contributor.authorVahokoski, Juhaen
dc.contributor.authorKursula, Petrien
dc.contributor.authorKursula, Inarien
dc.date.accessioned2016-03-24T12:01:45Zen
dc.date.available2016-03-24T12:01:45Zen
dc.date.issued2012en
dc.identifier.citationThe lasso segment is required for functional dimerization of the Plasmodium formin 1 FH2 domain. 2012, 7 (3):e33586 PLoS ONEen
dc.identifier.issn1932-6203en
dc.identifier.pmid22428073en
dc.identifier.doi10.1371/journal.pone.0033586en
dc.identifier.urihttp://hdl.handle.net/10033/603604en
dc.description.abstractApicomplexan parasites, such as the malaria-causing Plasmodium species, utilize a unique way of locomotion and host cell invasion. This substrate-dependent gliding motility requires rapid cycling of actin between the monomeric state and very short, unbranched filaments. Despite the crucial role of actin polymerization for the survival of the malaria parasite, the majority of Plasmodium cellular actin is present in the monomeric form. Plasmodium lacks most of the canonical actin nucleators, and formins are essentially the only candidates for this function in all Apicomplexa. The malaria parasite has two formins, containing conserved formin homology (FH) 2 and rudimentary FH1 domains. Here, we show that Plasmodium falciparum formin 1 associates with and nucleates both mammalian and Plasmodium actin filaments. Although Plasmodium profilin alone sequesters actin monomers, thus inhibiting polymerization, its monomer-sequestering activity does not compete with the nucleating activity of formin 1 at an equimolar profilin-actin ratio. We have determined solution structures of P. falciparum formin 1 FH2 domain both in the presence and absence of the lasso segment and the FH1 domain, and show that the lasso is required for the assembly of functional dimers.en
dc.language.isoenen
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/226716en
dc.rightsopenAccessen
dc.subject.meshActinsen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshCircular Dichroismen
dc.subject.meshCloning, Molecularen
dc.subject.meshDimerizationen
dc.subject.meshFetal Proteinsen
dc.subject.meshLocomotionen
dc.subject.meshMicrofilament Proteinsen
dc.subject.meshModels, Molecularen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshNuclear Proteinsen
dc.subject.meshPlasmodium falciparumen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshScattering, Small Angleen
dc.titleThe lasso segment is required for functional dimerization of the Plasmodium formin 1 FH2 domain.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, University of Hamburg, and German Electron Synchrotron (DESY), Hamburg, Germany.en
dc.identifier.journalPloS oneen

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