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Strong Binding of Myosin Heads Stretches and Twists the Actin Helix

Andrey K. Tsaturyan ^*, Natalia Koubassova ^*, Michael A. Ferenczi , Theyencheri Narayanan , Manfred Roessle  and Sergey Y. Bershitsky 

^* Institute of Mechanics, M. V. Lomonosov Moscow State University, Moscow, Russia; Biomedical Sciences Division, Imperial College, London, United Kingdom; European Synchrotron Radiation Facility, Grenoble, France; and Institute of Immunology and Physiology, Ural Branch of the Russian Academy of Sciences, Yekaterinburg, Russia

Correspondence: Address reprint requests to Sergey Y. Bershitsky, Institute of Immunology and Physiology, Ural Branch of the Russian Academy of Sciences, Rm. 325, 91 Pervomayskaya ul., Yekaterinburg 620219, Russia. Tel.: 7-343-374-1316; Fax: 7-343-374-0070; E-mail: syb{at}efif.uran.ru.

Calculation of the size of the power stroke of the myosin motor in contracting muscle requires knowledge of the compliance of the myofilaments. Current estimates of actin compliance vary significantly introducing uncertainty in the mechanical parameters of the motor. Using x-ray diffraction on small bundles of permeabilized fibers from rabbit muscle we show that strong binding of myosin heads changes directly the actin helix. The spacing of the 2.73-nm meridional x-ray reflection increased by 0.22% when relaxed fibers were put into low-tension rigor (<10 kN/m²) demonstrating that strongly bound myosin heads elongate the actin filaments even in the absence of external tension. The pitch of the 5.9-nm actin layer line increased by 0.62% and that of the 5.1-nm layer line decreased by 0.26%, suggesting that the elongation is accompanied by a decrease in its helical angle (166°) by 0.8°. This effect explains the difference between actin compliance revealed from mechanical experiments with single fibers and from x-ray diffraction on whole muscles. Our measurement of actin compliance obtained by applying tension to fibers in rigor is consistent with the results of mechanical measurements.

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