The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
25 03 2021
Historique:
received: 10 11 2020
accepted: 08 02 2021
entrez: 26 3 2021
pubmed: 27 3 2021
medline: 10 4 2021
Statut: epublish

Résumé

Plasmodium falciparum, the causative agent of malaria, moves by an atypical process called gliding motility. Actomyosin interactions are central to gliding motility. However, the details of these interactions remained elusive until now. Here, we report an atomic structure of the divergent Plasmodium falciparum actomyosin system determined by electron cryomicroscopy at the end of the powerstroke (Rigor state). The structure provides insights into the detailed interactions that are required for the parasite to produce the force and motion required for infectivity. Remarkably, the footprint of the myosin motor on filamentous actin is conserved with respect to higher eukaryotes, despite important variability in the Plasmodium falciparum myosin and actin elements that make up the interface. Comparison with other actomyosin complexes reveals a conserved core interface common to all actomyosin complexes, with an ancillary interface involved in defining the spatial positioning of the motor on actin filaments.

Identifiants

pubmed: 33767187
doi: 10.1038/s41467-021-22093-4
pii: 10.1038/s41467-021-22093-4
pmc: PMC7994445
doi:

Substances chimiques

Actins 0
Protozoan Proteins 0
Actomyosin 9013-26-7
Myosins EC 3.6.4.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1892

Subventions

Organisme : NIAID NIH HHS
ID : R01 AI132378
Pays : United States
Organisme : NIH HHS
ID : S10 OD012372
Pays : United States
Organisme : NIH HHS
ID : S10 OD026926
Pays : United States

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Auteurs

Julien Robert-Paganin (J)

Structural Motility, Institut Curie, CNRS, UMR 144, Paris, France.

Xiao-Ping Xu (XP)

Scintillon Institute, San Diego, CA, USA.

Mark F Swift (MF)

Scintillon Institute, San Diego, CA, USA.

Daniel Auguin (D)

Structural Motility, Institut Curie, CNRS, UMR 144, Paris, France.
Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC), Université d'Orléans, INRAE, USC1328, Orléans, France.

James P Robblee (JP)

Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT, USA.

Hailong Lu (H)

Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT, USA.

Patricia M Fagnant (PM)

Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT, USA.

Elena B Krementsova (EB)

Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT, USA.

Kathleen M Trybus (KM)

Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT, USA.

Anne Houdusse (A)

Structural Motility, Institut Curie, CNRS, UMR 144, Paris, France. anne.houdusse@curie.fr.

Niels Volkmann (N)

Scintillon Institute, San Diego, CA, USA. niels.volkmann@pasteur.fr.
Structural Image Analysis Unit, Department of Structural Biology & Chemistry, Institut Pasteur, Paris, France. niels.volkmann@pasteur.fr.

Dorit Hanein (D)

Scintillon Institute, San Diego, CA, USA.
Structural Studies of Macromolecular Machines in Cellulo Unit, Department of Structural Biology & Chemistry, Institut Pasteur, Paris, France.

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Classifications MeSH