Muscle force is generated by myosin heads stereospecifically attached to actin
Sergey Y. Bershitsky,
Andrey K. Tsaturyan,
Olga N. Bershitskaya,
Gregory I. Mashanov,
Paul Brown,
Ronald Burns and
Michael A. Ferenczi ()
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Sergey Y. Bershitsky: *Institute of Physiology, Urals Branch of the Russian Academy of Sciences
Andrey K. Tsaturyan: †Institute of Mechanics, Lomonosov Moscow University
Olga N. Bershitskaya: *Institute of Physiology, Urals Branch of the Russian Academy of Sciences
Gregory I. Mashanov: *Institute of Physiology, Urals Branch of the Russian Academy of Sciences
Paul Brown: National Institute for Medical Research
Ronald Burns: National Institute for Medical Research
Michael A. Ferenczi: National Institute for Medical Research
Nature, 1997, vol. 388, issue 6638, 186-190
Abstract:
Abstract Muscle force is generated by myosin crossbridges interacting with actin. As estimated from stiffness1,2 and equatorial X-ray diffraction3 of muscle and muscle fibres, most myosin crossbridges are attached to actin during isometric contraction, but a much smaller fraction is bound stereospecifically4,5,6,7. To determine the fraction of crossbridges contributing to tension and the structural changes that attached crossbridges undergo when generating force, we monitored the X-ray diffraction pattern during temperature-induced tension rise in fully activated permeabilized frog muscle fibres. Temperature jumps8 from 5–6 °C to 16–19 °C initiated a 1.7-fold increase in tension without significantly changing fibre stiffness or the intensities of the (1,1) equatorial and (14.5 nm)−1 meridional X-ray reflections. However, tension rise was accompanied by a 20% decrease in the intensity of the (1,0) equatorial reflection and an increase in the intensity of the first actin layer line by ∼13% of that in rigor. Our results show that muscle force is associated with a transition of the crossbridges from a state in which they are nonspecifically attached to actin to one in which stereospecifically bound myosin crossbridges label the actin helix.
Date: 1997
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DOI: 10.1038/40651
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