来自盘基网柄菌的一种40000道尔顿的蛋白质以钙离子依赖的方式影响肌动蛋白的组装特性。
A 40,000-dalton protein from Dictyostelium discoideum affects assembly properties of actin in a Ca2+-dependent manner.
作者信息
Brown S S, Yamamoto K, Spudich J A
出版信息
J Cell Biol. 1982 Apr;93(1):205-10. doi: 10.1083/jcb.93.1.205.
Abstract
A 40,000-dalton protein that affects the assembly properties of actin in a Ca2+-dependent manner has been purified from Dictyostelium discoideum. Gel filtration chromatography indicates that the native form of this protein is a monomer. A major effect of this protein is to reduce the sedimentability of F-actin in a stoichiometric fashion. Nearly complete loss of sedimentability is observed at ratios of the 40,000-dalton protein to actin of greater than 1:10. At low stoichiometries, this protein can accelerate the rate of actin assembly under certain experimental conditions. These effects of the 40,000-dalton protein on the actin assembly properties described above require calcium ion. The 40,000-dalton protein does not exert its effects by proteolyzing actin. Furthermore, peptide maps demonstrate that this protein is not a proteolytic fragment of actin.
摘要
一种分子量为40000道尔顿的蛋白质已从盘基网柄菌中纯化出来，它以钙离子依赖的方式影响肌动蛋白的组装特性。凝胶过滤色谱法表明该蛋白质的天然形式是单体。这种蛋白质的主要作用是以化学计量的方式降低F-肌动蛋白的沉降能力。当40000道尔顿蛋白质与肌动蛋白的比例大于1:10时，几乎完全丧失沉降能力。在低化学计量比时，在某些实验条件下这种蛋白质可以加速肌动蛋白的组装速率。上述40000道尔顿蛋白质对肌动蛋白组装特性的这些影响需要钙离子。40000道尔顿蛋白质不是通过蛋白水解肌动蛋白来发挥作用的。此外，肽图表明这种蛋白质不是肌动蛋白的蛋白水解片段。
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