Fukui Y
J Cell Biol. 1978 Jan;76(1):146-57. doi: 10.1083/jcb.76.1.146.
Electron microscopic evidence demonstrated that dimethyl sulfoxide (DMSO) induces formation of giant intranuclear microfilament bundles in the interphase nucleus of a cellular slime mold, Dictyostelium. These giant bundles are approximately giant bundles are approximately 3 micrometer long, 0.85 micrometer wide, and composed of microfilaments 6 nm in diameter. Studies in which glycerinated cells were used showed that these microfilaments bind rabbit skeletal muscle heavy meromyosin, forming typical decorated "arrowhead" structures, and that this binding can be reverted by Mg-adenosine triphosphate. These data verify that the intranuclear microfilaments are the contractile protein actin, and that DMSO affects intranuclear actin, inducing the formation of such giant bundles. The intranuclear actin bundles appear at any developmental stage in two different species of cellular slime molds after treatment with DMSO. The native form of the intranuclear actin molecules and their possible functions are discussed, and it is proposed that the contractile protein has essential functions in the cell nucleus.
电子显微镜证据表明,二甲基亚砜(DMSO)可诱导细胞黏菌盘基网柄菌间期细胞核内形成巨大的核内微丝束。这些巨大的微丝束长度约为3微米,宽度约为0.85微米,由直径6纳米的微丝组成。使用甘油处理细胞的研究表明,这些微丝能结合兔骨骼肌重酶解肌球蛋白,形成典型的带装饰的“箭头”结构,并且这种结合可被三磷酸镁腺苷逆转。这些数据证实核内微丝是收缩蛋白肌动蛋白,且DMSO影响核内肌动蛋白,诱导形成此类巨大的微丝束。在用DMSO处理后,核内肌动蛋白束在两种不同的细胞黏菌的任何发育阶段都会出现。文中讨论了核内肌动蛋白分子的天然形式及其可能的功能,并提出收缩蛋白在细胞核中具有重要功能。