Maruyama K
J Biol Chem. 1981 Feb 10;256(3):1060-2.
Polymerization of actin was completely inhibited by metal chelating agents, such as EDTA or diaminocyclohexanetetraacetic acid, even in the presence of 0.1 M KCl and excess ATP. Addition of 1 mM MgCl2, but not CaCl2, caused full polymerization in the presence of 10 mM diaminocyclohexanetetraacetic acid, suggesting that micromolar concentrations of Mg ions are required for the polymerization of actin. However, it turned out that sonic vibration induced a very rapid polymerization of actin in the absence of Mg ions. The sonication-induced polymerization of actin was greatly inhibited by cytochalasins D and B, and partially by beta-actinin. This can be explained by assuming that the fast growing ends of the formed nuclei are blocked by the cytochalasins, and the slowly growing ends with beta-actinin. The elongation of added F-actin fragments was also similarly inhibited by the cytochalasins and beta-actinin in the absence of Mg ions. It appears that sonic vibration enhances nuclei formation of actin monomers by mechanical agitation in the absence of Mg ions, which stabilize formed nuclei.
肌动蛋白的聚合完全被金属螯合剂(如EDTA或二氨基环己烷四乙酸)抑制,即使存在0.1 M KCl和过量ATP。添加1 mM MgCl2而非CaCl2,在存在10 mM二氨基环己烷四乙酸的情况下会导致完全聚合,这表明微摩尔浓度的镁离子是肌动蛋白聚合所必需的。然而,结果表明,在没有镁离子的情况下,超声振动会诱导肌动蛋白非常快速地聚合。超声诱导的肌动蛋白聚合受到细胞松弛素D和B的极大抑制,部分受到β - 辅肌动蛋白的抑制。这可以通过假设形成的核的快速生长末端被细胞松弛素阻断,而缓慢生长末端被β - 辅肌动蛋白阻断来解释。在没有镁离子的情况下,添加的F - 肌动蛋白片段的伸长也同样受到细胞松弛素和β - 辅肌动蛋白的抑制。似乎超声振动在没有镁离子的情况下通过机械搅拌增强了肌动蛋白单体的核形成,而镁离子可稳定形成的核。