离心显微镜下巨藻细胞超快速肌动蛋白-肌球蛋白滑动产生细胞质流动的机制研究

S. Chaen, H. Sugi
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引用次数: 0

摘要

在绿藻Chara collaria的巨型多式联运细胞中,细胞质流动是由atp依赖的肌球蛋白头和固定在叶绿体上的肌动蛋白丝阵列(肌动蛋白线)之间的滑动产生的。细胞质流动的速度比骨骼肌肌丝最大滑动速度快许多倍。在本文中,我们使用离心显微镜比较了细胞质肌凝蛋白与骨骼肌和心肌肌凝蛋白之间的稳态力-速度(P-V)关系,在离心显微镜下,使肌凝蛋白包被的乳胶珠在不同的离心力下沿着肌动蛋白电缆滑动。与肌动蛋白-肌球蛋白在骨骼和心脏肌动蛋白滑移的双曲P-V关系相反,细胞质肌动蛋白与肌动蛋白索滑移的P-V关系是一条直线,表明占空比非常大,化学能转换率非常小。讨论了超快速肌动蛋白-肌球蛋白滑动的可能机制。•由巨藻细胞中肌凝蛋白和肌动蛋白之间的atp依赖性滑动引起的细胞质流的速度比骨骼肌和心肌中atp依赖性肌动蛋白-肌凝蛋白滑动快许多倍。•利用离心显微镜研究了超快速肌动蛋白-肌球蛋白滑动的机制,其中使涂有细胞质肌球蛋白的微球在不同的离心力下沿着肌动蛋白电缆滑动,作为细胞质肌动蛋白与肌动蛋白电缆滑动的负载。•与骨骼肌和心肌肌动蛋白-肌球蛋白滑动的双曲力-速度(P-V)关系不同,细胞质肌动蛋白-肌球蛋白滑动的P-V关系是一条直线,而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,化学-机械能转换的占空比非常大,效率非常低。
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Mechanism of Ultra-Fast Actin-Myosin Sliding Producing Cytoplasmic Streaming in Giant Algal Cell, Studied Using the Centrifuge Microscope
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.
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