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The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
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Unconventional Imaging Methods to Capture Transient Structures during Actomyosin Interaction.

Eisaku Katayama1, Noriyuki Kodera2,3

  • 1Waseda Research Institute for Science and Engineering, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan. ekatayam2008@gmail.com.

International Journal of Molecular Sciences
|May 9, 2018
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Summary
This summary is machine-generated.

New microscopy techniques reveal novel myosin head configurations, revising our understanding of the muscle cross-bridge mechanism. These methods offer insights into transient protein structures crucial for muscle tension generation.

Keywords:
actincryo-electron microscopyhigh-speed atomic-force microscopylever-arm swingingmyosin cross-bridgesmyosin subdomainsmyosin-IImyosin-Vquick-freeze deep-etch replica electron microscopystructural intermediate

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • The cross-bridge structure is the molecular basis of muscle tension.
  • Understanding transient configurations of myosin heads remains challenging due to their size and rapid movement.

Purpose of the Study:

  • To investigate the structural dynamics of myosin heads during muscle contraction.
  • To explore unconventional microscopy methods for visualizing transient protein structures.

Main Methods:

  • Quick-freeze deep-etch-replica electron microscopy (FDER-EM) applied to in vitro motility assays.
  • High-speed atomic-force microscopy (HS-AFM) for observing protein assembly dynamics.
  • Integration of biochemical and biophysical data.

Main Results:

  • FDER-EM revealed novel myosin head configurations similar to SH1-SH2-crosslinked myosin.
  • HS-AFM visualized myosin-V movement, showing behaviors like 'foot-stomping' and tail unwinding.
  • A revised cross-bridge mechanism incorporating a new conformer was proposed.

Conclusions:

  • Unconventional microscopy methods provide valuable insights into transient protein structures.
  • Novel myosin head conformations play a key role in the revised cross-bridge mechanism.
  • These techniques advance our understanding of molecular motors and muscle function.