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首页> 外文期刊>Journal of Material Sciences & Engineering >Mechanism of Ultra-Fast Actin-Myosin Sliding Producing Cytoplasmic Streaming in Giant Algal Cell, Studied Using the Centrifuge Microscope
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Mechanism of Ultra-Fast Actin-Myosin Sliding Producing Cytoplasmic Streaming in Giant Algal Cell, Studied Using the Centrifuge Microscope

机译:用离心显微镜研究超快速肌动蛋白-肌球蛋白滑动产生巨藻细胞胞质流的机理

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In giant intermodal cells of green algae Chara collaria, cytoplasmic streaming is produced by ATP-dependent sliding between myosin heads extending from amorphous cytoplasmic organelles and actin filament arrays (actin cables) fixed on chloroplast rows. The velocity of cytoplasmic streaming is many times faster than the maximum myofilament sliding in skeletal muscle. In this article, we compared steady-state force-velocity (P-V) relations between cytoplasmic myosin and skeletal and cardiac muscle myosins using the centrifuge microscope, in which myosincoated latex beads were made to slide along the actin cables under various centrifugal forces. In contrast with the hyperbolic P-V relation of actin-myosin sliding in skeletal and cardiac myosins, the P-V relation of cytoplasmic myosin versus actin cable sliding was a straight line, indicating a very large duty ratio and a very small rate of chemomechanical energy conversion. Possible mechanisms of the ultra-fast actin-myosin sliding are discussed.Highlights• The velocity of cytoplasmic streaming, caused by ATP-dependent sliding between cytoplasmic myosin and actin cables in giant algal cells is many times faster than ATP-dependent actin-myosin sliding in skeletal and cardiac muscles.• The mechanism of ultra-fast actin-myosin sliding was studied using the centrifuge microscope, in which beads coated with cytoplasmic myosin were made to slide along actin cables under various centrifugal forces serving as loads against cytoplasmic myosin versus actin cable sliding.• Unlike the hyperbolic force-velocity (P-V) relation of skeletal and cardiac muscle actin-myosin sliding, the P-V relation of cytoplasmic actin myosin sliding was a straight line irrespective of the force generated by cytoplasmic myosin.• These results indicate a very large duty ratio and a very small efficiency of chemo-mechanical energy conversion in cytoplasmic actin-myosin sliding.
机译:在绿藻Chara ringia的巨型联运细胞中,细胞质流是通过从无定形细胞质细胞器延伸的肌球蛋白头与固定在叶绿体行上的肌动蛋白丝阵列(肌动蛋白电缆)之间的ATP依赖性滑动产生的。细胞质流的速度比骨骼肌中最大肌丝滑动的速度快许多倍。在本文中,我们使用离心显微镜比较了细胞质肌球蛋白与骨骼肌和心肌肌球蛋白之间的稳态力-速度(P-V)关系,其中在不同的离心力作用下,肌球蛋白包裹的乳胶珠沿着肌动蛋白电缆滑动。与肌动蛋白-肌球蛋白在骨骼肌和心肌肌球蛋白中滑行的双曲线P-V关系相反,细胞质肌球蛋白与肌动蛋白电缆滑行的P-V关系呈直线,表明占空比非常大,化学机械能转换率非常小。讨论了超快速肌动蛋白-肌球蛋白滑动的可能机制。要点•巨藻细胞中胞质肌球蛋白和肌动蛋白电缆之间的ATP依赖性滑动引起的胞质流速度比ATP依赖性肌动蛋白-肌球蛋白滑动快许多倍。 •使用离心显微镜研究肌动蛋白-肌球蛋白超快滑动的机制,其中使涂有细胞质肌球蛋白的珠子在各种离心力作用下沿着肌动蛋白电缆滑动,以抵抗细胞质肌球蛋白与肌动蛋白的负荷。 •与骨骼肌和肌动蛋白-肌球蛋白滑动的双曲线力-速度(PV)关系不同,胞质肌动蛋白-肌球蛋白滑动的PV关系是一条直线,与细胞质肌球蛋白产生的力无关。•这些结果表明,在细胞质肌动蛋白-肌球蛋白滑动中,非常大的占空比和非常小的化学机械能转换效率。

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