1. The excluded volume effect induced by poly(ethylene glycol) modulates the motility of actin filaments interacting with myosin.
- Author
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Munakata S and Hatori K
- Subjects
- Actin Cytoskeleton chemistry, Actomyosin chemistry, Actomyosin drug effects, Actomyosin metabolism, Adenosine Triphosphate metabolism, Animals, Biophysical Phenomena, Models, Molecular, Molecular Motor Proteins chemistry, Molecular Motor Proteins drug effects, Molecular Motor Proteins metabolism, Molecular Weight, Muscle, Skeletal chemistry, Myosin Subfragments chemistry, Myosin Subfragments drug effects, Myosin Subfragments metabolism, Myosins chemistry, Osmotic Pressure, Polyethylene Glycols chemistry, Rabbits, Tropomyosin chemistry, Tropomyosin drug effects, Tropomyosin metabolism, Troponin chemistry, Troponin drug effects, Troponin metabolism, Actin Cytoskeleton drug effects, Actin Cytoskeleton metabolism, Myosins drug effects, Myosins metabolism, Polyethylene Glycols pharmacology
- Abstract
To examine the motility of actomyosin complexes in the presence of high concentrations of polymers, we investigated the effect of poly(ethylene glycol) on the sliding velocities of actin filaments and regulated thin filaments on myosin molecules in the presence of ATP. Increased concentrations and relative molecular masses of poly(ethylene glycol) decreased the sliding velocities of actin and regulated thin filaments. The decreased ratio of velocity in regulated thin filaments at - log[Ca(2+) ] of 4 was higher than that of actin filaments. Furthermore, in the absence of Ca(2+) , regulated thin filaments were moderately motile in the presence of poly(ethylene glycol). The excluded volume change (∆V), defined as the change in water volume surrounding actomyosin during the interactions, was estimated by determining the relationship between osmotic pressure exerted by poly(ethylene glycol) and the decreased ratio of the velocities in the presence and absence of poly(ethylene glycol). The ∆V increased up to 3.7 × 10(5) Å(3) as the Mr range of poly(ethylene glycol) was increased up to 20,000. Moreover, the ∆V for regulated thin filaments was approximately two-fold higher than that of actin filaments. This finding suggests that differences in the conformation of filaments according to whether troponin-tropomyosin complexes lie on actin filaments alter the ∆V during interactions of actomyosin complexes and influence motility., (© 2013 FEBS.)
- Published
- 2013
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