In vitro motility of skeletal muscle myosin and its proteolytic fragments.

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概要

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• We have compared actin-activated myosin ATPase activity, myosin binding to actin, and the velocity of myosin-induced actin sliding in order to understand the mechanism of myosin motility. In our in vitro assay, F-actin slides at a constant velocity, regardless of length. The F-actin could slide over myosin heads at KC1 concentrations below a critical value (60mM with myosin and HMM, 100mM with S-1), and the sliding velocities were quite similar below the critical KC1 concentration. However, at KC1 concentrations close to the critical value, the sliding F-actin is attached to only one or a few particular points on the surface, each of which perhaps consists of a single head of myosin. The KATPase values for actin-activated ATPase were_??_30μM for S-1 and _??_200μM with HMM below the critical KC1 concentration, and _??_5, 000μM above the critical KC1 concentration. This increase in KATpase is due to a drastic reduction in the binding affinity of myosin heads to F-actin, as determined by a proteolytic digestion method and direct observation by fluorescence microscopy. We also show that the Vmax of actin-activated myosin ATPase activity decreases steadily with increasing KC1 concentration, even though the velocity of F-actin sliding remains unchanged. This result provides evidence that the ATPase activity is not necessarily linked to motility. We discuss possible models that do not require a tight coupling between myosin ATPase and motility.

• 社団法人 日本生化学会の論文

著者

• Hayashi Hiroshi

  Department of Biomolecular Science, Faculty of Science, Toho University

• Takiguchi Kingo

  Department Of Molecular Biology And Biochemistry Busch Campus Rutgers University Piscataway

• Kurimoto Eiji

  Department Of Applied Physics Osaka University

• HIGASHI-FUJIME Sugie

  Department of Molecular Biology, Faculty of Science, Nagoya University

• Kurimoto Eiji

  Department of Molecular Biology, Faculty of Science, Nagoya University

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• In vitro motility of skeletal muscle myosin and its proteolytic fragments.

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