title: The excluded volume effect induced by poly(ethylene glycol) modulates the motility of actin filaments interacting with myosin.
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.
authors.affiliation: Department of Bio-Systems Engineering, Graduate School of Science and Engineering, Yamagata University, Yonezawa, Japan.
authors.forename: Shinsuke
authors.initials: S
authors.lastname: Munakata
authors.forename: Kuniyuki
authors.initials: K
authors.lastname: Hatori
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism*; D000205:Actomyosin / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D055592:Biophysical Phenomena; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D008970:Molecular Weight; D018482:Muscle, Skeletal / Q000737:chemistry; D015879:Myosin Subfragments / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D009218:Myosins / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism*; D009997:Osmotic Pressure; D011092:Polyethylene Glycols / Q000737:chemistry / Q000494:pharmacology*; D011817:Rabbits; D014335:Tropomyosin / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D014336:Troponin / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism
chemical_list: D020409:Molecular Motor Proteins; D015879:Myosin Subfragments; D014335:Tropomyosin; D014336:Troponin; D011092:Polyethylene Glycols; D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins
keywords: Ca2+ regulation; in vitro motility assay; muscle protein; osmotic pressure; preferential hydration