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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Actins from plant and animal sources tend not to form heteropolymers in vitro and function differently in plant cells
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Actins from plant and animal sources tend not to form heteropolymers in vitro and function differently in plant cells

机译：来自动植物的肌动蛋白往往不会在体外形成杂聚物，并且在植物细胞中的功能不同

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Pollen and skeletal muscle actins were purified and labeled with fluorescent dyes that have different emission wavelengths. Observation by electron microscopy shows that the fluorescent actins are capable to polymerize into filamentous actin in vitro, bind to myosin S-1 fragments, and have a critical concentration similar to unlabeled actin, indicating that they are functionally active. The globular actins from two sources were mixed and polymerized by the addition of ATP and salts. The copolymerization experiment shows that when excited by light of the appropriate wavelength, both red actin filaments (pollen actin) and green actin filaments (muscle actin) can be visualized under the microscope, but no filaments exhibiting both green and red colors are detected. Furthermore, coprecipitations of labeled pollen actin with unlabeled pollen and skeletal muscle actin were performed. Measurements of fluorescent intensity show that the amount of labeled pollen actin precipitating with pollen actin was much higher than that with skeletal muscle actin, indicating that pollen and muscle actin tend not to form heteropolymers. Injection of labeled pollen actin into living stamen hair cells results in the formation of normal actin filaments in transvacuolar strands and the cortical cytoplasm. In contrast, labeled skeletal muscle actin has detrimental effects on the cellular architecture. The results from coinjection of the actin-disrupting reagent cytochalasin D with pollen actin show that overexpression of pollen actin prolongs the displacement of the nucleus and facilitates the recovery of the nuclear position, actin filament architecture, and transvacuolar strands. However, muscle actin perturbs actin filaments when injected into stamen hair cells. Moreover, nuclear displacement occurs more rapidly when cytochalasin D and muscle actin are coinjected into the cell. It is concluded that actins from plant and animal sources behave differently in vitro and in vivo and that they are functionally not interchangeable. [References: 25]
机译：纯化花粉和骨骼肌肌动蛋白，并用具有不同发射波长的荧光染料标记。电子显微镜观察表明，荧光肌动蛋白能够在体外聚合成丝状肌动蛋白，与肌球蛋白S-1片段结合，并具有与未标记肌动蛋白相似的临界浓度，表明它们具有功能活性。通过添加ATP和盐将两种来源的球状肌动蛋白混合并聚合。共聚实验表明，当被适当波长的光激发时，红色肌动蛋白丝（花粉肌动蛋白）和绿色肌动蛋白丝（肌肉肌动蛋白）都可以在显微镜下观察到，但没有发现绿色和红色的丝。此外，进行了标记花粉肌动蛋白与未标记花粉和骨骼肌肌动蛋白的共沉淀。荧光强度的测量表明，花粉肌动蛋白沉淀的标记花粉肌动蛋白的量比骨骼肌肌动蛋白沉淀的高得多，表明花粉和肌动蛋白倾向于不形成杂聚物。将标记的花粉肌动蛋白注射到活的雄蕊毛细胞中会导致正常的肌动蛋白丝在透真空链和皮质细胞质中形成。相反，标记的骨骼肌肌动蛋白对细胞结构具有有害作用。破坏肌动蛋白的试剂细胞松弛素D与花粉肌动蛋白的共同注射的结果表明，花粉肌动蛋白的过表达延长了细胞核的移位，并促进了核位置，肌动蛋白丝结构和跨真空链的恢复。但是，肌动蛋白注射到雄蕊毛细胞中会干扰肌动蛋白丝。此外，当细胞松弛素D和肌肉肌动蛋白共同注入细胞时，核移位发生得更快。结论是，动植物来源的肌动蛋白在体外和体内表现不同，并且在功能上不可互换。 [参考：25]

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