Growth of synthetic myosin filaments from myosin minifilaments.
Growth of synthetic myosin filaments from myosin minifilaments.
复制标题
从肌球蛋白微丝生长合成肌球蛋白丝。
DOI：
10.1021/bi00533a018
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
Lake,JA
中科院分区：
文献类型：
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作者：
Reisler,E;Cheung,P;Oriol-Audit,C;Lake,JA
Emil Reisler，* Pearl Cheung，克莉丝汀Oriol-Audit，1和James A. Lake摘要：将KCl加入到10 mM柠檬酸盐-Tris缓冲液（pH 8.0）中的合成肌球蛋白微丝溶液中，诱导细丝生长。这些细丝在pH 8.0时，在形态和流体动力学性质上类似于Josephs和哈灵顿所述的合成絮凝剂[Josephs，R.，&哈灵顿，W. F.（1966）Biochemistry 5，3474-3487]，细丝生长的速率关键地取决于溶液中的KCl浓度。在低浓度（低于80 mM KCl）和高浓度（高于0. 15 Mkc 1）盐浓度下，而在中间KCl浓度下，细丝以快的速率形成。由微纤丝形成纤丝是一个可逆的过程，在中等盐浓度下，这两种聚合物体系似乎处于动态平衡。少量的微丝可以诱导游离肌球蛋白的快速聚合，即它们可以作为种子材料。这些和其他意见进行了讨论，从肌球蛋白微丝的长丝形成的直接途径。Huxley（1963）的电子显微镜研究证实了天然肌球蛋白细丝和通过降低肌球蛋白溶液的离子强度获得的合成细丝的结构相似性。这些发现意味着同样的原理可能支配着两种纤维的组装。肌球蛋白丝的双极特征，以及肌球蛋白丝的存在，
Emil Reisler,* Pearl Cheung, Christine Oriol-Audit, 1 and James A. Lake abstract: Addition of KC1 to a solution of synthetic myosin minifilaments in 10 mM citrate-Tris buffer (pH 8.0) induces the growth of filaments. These filaments, at pH 8.0, resemble in their morphological and hydrodynamic properties the syn-thetic filamentsdescribed by Josephs and Harrington [Josephs, R., & Harrington, W. F.(1966) Biochemistry 5, 3474-3487], The rate of filament growth depends critically on the KC1 concentration in the solution. Low rates of filament formation are noted in the presence of both low (below 80 mM KC1) and high (above0. 15 Mkc1) salt concentrations, whereas at the intermediate KC1 concentrations the filaments are formed at a fast rate. The formation of filaments from minifilaments is a reversible process, and under moderate salt concentrations, these twopolymeric systems appear to existin a dynamic equilibrium. Small amounts of minifilaments can induce rapid polymerization of dissociated myosin; ie, they can act as a seeding material. These and other observations are discussed in terms of a direct route for filament formation from myosin minifilaments. e electron microscopy studies of Huxley (1963) established the structural similarities of native myosin filaments and the synthetic filaments obtained by decreasing the ionic strength of a myosin solution. These findings implied that the same principles might govern the assembly of both filaments. The bipolar character of myosin filaments, and the presence of a