Switching of actin-myosin motors by voltage-induced pH bias in vitro

Hatori, Kuniyuki; Iwase, Takahiro; Wada, Reito

doi:10.1016/j.abb.2016.05.012

Cited by 3 publications

(1 citation statement)

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“…The microscopic images (1 byte gray scale) were obtained using a CCD camera (WAT‐910HXN; Watec Co., Ltd., Yamagata, Japan) at intervals of 1/15 s. The velocity of the moving filaments was determined by measuring the displacements in successive images at intervals of 1/15 s with a customized program. [ 50 ] The fraction of moving filaments was defined as the percentage of the number of moving filaments over all observed filaments at an interval of 20 s on a view field (58 × 44 µm).…”

Section: Methodsmentioning

confidence: 99%

Polymer‐Carrying Ability of Actin Filaments Interacting with Myosin Motors in a Biological Motility System In Vitro

Sunada

Hatori

2022

Macromolecular Bioscience

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The reconstituted motility system of actin-myosin is expected to be used in bioinspired transport devices, in which carried materials are attached to either moving actin filaments or walking myosin molecules. However, the dependence of the ability to transport on the size of the attached materials is still inadequately understood. Here, as carried materials, polyethylene glycols (PEGs) of various sizes are covalently bound to actin filaments, and the motility of PEG-attached filaments on a heavy meromyosin (HMM) immobilized on a glass surface is observed via fluorescence microscopy. Full attachment of 2 kDa PEG, with an approximately 2 nm gyration radius, decreases the velocity and fraction of moving actin filaments by approximately 10% relative to unattached filaments. For the 5 kDa PEG, the fraction of moving filaments is decreased by approximately 70% even when the filaments contain only 20% PEG-attached actin. The attachment of both sizes of PEGs suppresses the actin-activated ATPase activity at the same level. These results suggest that actin filaments can carry PEGs up to 2 kDa having the same size as actin monomers, while the rate of ATP hydrolysis is limited. The size dependence may provide a criterion for material delivery via actin filaments in nanotransport applications.

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Section: Methodsmentioning

confidence: 99%