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首页> 外文期刊>Biochemistry >ROLE OF THE DICTYOSTELIUM 30 KDA PROTEIN IN ACTIN BUNDLE FORMATION
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ROLE OF THE DICTYOSTELIUM 30 KDA PROTEIN IN ACTIN BUNDLE FORMATION

机译：DICTYOSTELIUM 30 KDA蛋白在ACTIN束形成中的作用

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摘要

We have studied the formation of bundles in mixtures of actin with the Dictyostelium 30 kDa actin-bundling protein as a function of 30 kDa protein concentration, actin concentration, and filament length. The presence of the 30 kDa protein promotes formation of filament bundles at actin concentrations and filament lengths that are not spontaneously aligned into liquid crystalline domains in the absence of the 30 kDa protein. Bundle formation in the presence of the 30 kDa protein was observed over a broad range of actin filament lengths and concentrations. Bundling was filament length dependent, and short filaments were more efficiently bundled. Bundles formed at actin concentrations as low as 2 mu M. The volume fraction of the bundled portion and concentrations of actin and the 30 kDa protein in the bundled portion were measured using a sedimentation assay. Bundles have concentrations of actin and 30 kDa protein that are 10-20 and 5-20 times, respectively, greater than that of the bulk solution. Computer modeling reveals that bundling of actin by a bundling protein increases both the mean length and the polydispersity of the length distribution, factors which lower the actin concentration required for spontaneous alignment within the bundle. We propose that entropy-driven spontaneous ordering may contribute to bundle formation in two ways. Bundling of actin creates longer aggregates with a more polydisperse length distribution in which actin aligns spontaneously within the bundle at very low concentrations. In addition, bundling creates locally high concentrations of actin within these aggregates that will spontaneously align, providing an additional driving force for bundle ordering.
机译：我们已经研究了肌动蛋白与Dictyostelium 30 kDa肌动蛋白捆绑蛋白的混合物中束的形成与30 kDa蛋白浓度，肌动蛋白浓度和细丝长度的关系。 30 kDa蛋白的存在促进了肌动蛋白浓度和丝长的细丝束的形成，而这些肌动蛋白的浓度和丝长在缺少30 kDa蛋白的情况下不会自发排列成液晶结构域。在广泛的肌动蛋白丝长度和浓度范围内观察到在30 kDa蛋白存在下的束形成。捆扎取决于长丝的长度，短的长丝更有效地捆扎。在肌动蛋白浓度低至2μM时形成的束。使用沉淀测定法测量束缚部分的体积分数以及束缚部分中肌动蛋白和30 kDa蛋白的浓度。束中肌动蛋白和30 kDa蛋白的浓度分别比本体溶液高10到20倍和5到20倍。计算机模型表明，通过束缚蛋白将肌动蛋白束缚会增加平均长度和长度分布的多分散性，这些因素会降低束中自发排列所需的肌动蛋白浓度。我们提出，熵驱动的自发有序可能以两种方式促进束的形成。肌动蛋白的捆绑产生更长的聚集体，具有更长的多分散长度分布，其中肌动蛋白以非常低的浓度自发排列在束中。另外，捆绑在这些聚集体中局部产生高浓度的肌动蛋白，这些肌动蛋白会自发排列，从而为捆绑订购提供了额外的驱动力。

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