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A myosin II nanomachine mimicking the striated muscle

Author

Listed:
  • Irene Pertici

    (University of Florence)

  • Lorenzo Bongini

    (University of Florence)

  • Luca Melli

    (University of Florence
    F. Hoffmann-La Roche Ltd)

  • Giulio Bianchi

    (University of Florence)

  • Luca Salvi

    (University of Florence
    University of Munich)

  • Giulia Falorsi

    (University of Florence)

  • Caterina Squarci

    (University of Florence)

  • Tamás Bozó

    (Semmelweis University)

  • Dan Cojoc

    (IOM-CNR)

  • Miklós S. Z. Kellermayer

    (Semmelweis University)

  • Vincenzo Lombardi

    (University of Florence)

  • Pasquale Bianco

    (University of Florence)

Abstract

The contraction of striated muscle (skeletal and cardiac muscle) is generated by ATP-dependent interactions between the molecular motor myosin II and the actin filament. The myosin motors are mechanically coupled along the thick filament in a geometry not achievable by single-molecule experiments. Here we show that a synthetic one-dimensional nanomachine, comprising fewer than ten myosin II dimers purified from rabbit psoas, performs isometric and isotonic contractions at 2 mM ATP, delivering a maximum power of 5 aW. The results are explained with a kinetic model fitted to the performance of mammalian skeletal muscle, showing that the condition for the motor coordination that maximises the efficiency in striated muscle is a minimum of 32 myosin heads sharing a common mechanical ground. The nanomachine offers a powerful tool for investigating muscle contractile-protein physiology, pathology and pharmacology without the potentially disturbing effects of the cytoskeletal—and regulatory—protein environment.

Suggested Citation

  • Irene Pertici & Lorenzo Bongini & Luca Melli & Giulio Bianchi & Luca Salvi & Giulia Falorsi & Caterina Squarci & Tamás Bozó & Dan Cojoc & Miklós S. Z. Kellermayer & Vincenzo Lombardi & Pasquale Bianco, 2018. "A myosin II nanomachine mimicking the striated muscle," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06073-9
    DOI: 10.1038/s41467-018-06073-9
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    Cited by:

    1. C. Arbore & M. Sergides & L. Gardini & G. Bianchi & A. V. Kashchuk & I. Pertici & P. Bianco & F. S. Pavone & M. Capitanio, 2022. "α-catenin switches between a slip and an asymmetric catch bond with F-actin to cooperatively regulate cell junction fluidity," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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