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

Julien Robert-Paganin, Xiao-Ping Xu, Mark F. Swift, Daniel Auguin, James P. Robblee, Hailong Lu, Patricia M. Fagnant, Elena B. Krementsova, Kathleen M. Trybus, Anne Houdusse (), Niels Volkmann () and Dorit Hanein
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Julien Robert-Paganin: Structural Motility, Institut Curie, CNRS, UMR 144
Xiao-Ping Xu: Scintillon Institute
Mark F. Swift: Scintillon Institute
Daniel Auguin: Structural Motility, Institut Curie, CNRS, UMR 144
James P. Robblee: University of Vermont
Hailong Lu: University of Vermont
Patricia M. Fagnant: University of Vermont
Elena B. Krementsova: University of Vermont
Kathleen M. Trybus: University of Vermont
Anne Houdusse: Structural Motility, Institut Curie, CNRS, UMR 144
Niels Volkmann: Scintillon Institute
Dorit Hanein: Scintillon Institute

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: Abstract 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.

Date: 2021
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DOI: 10.1038/s41467-021-22093-4

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