Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium.
Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium.
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三种肌动蛋白交联蛋白，即 34 kDa 肌动蛋白捆绑蛋白、α-肌动蛋白和凝胶因子 (ABP-120)，在盘基网柄菌的生长和发育中具有独特和冗余的作用。
作者：
Francisco Rivero;R. Furukawa;M. Fechheimer;A. A. Noegel
在三种单突变体（αA-、120-和 34-）和三种双突变体（αA-/120-、34-/alphaA-、34-/120-）菌株中研究了三种肌动蛋白交联蛋白、α-肌动蛋白（alphaA）、胶凝因子（ABP-120）和 34 kDa 肌动蛋白捆绑蛋白对细胞功能的贡献。通过同源重组产生盘基网柄菌。菌株 alphaA-/120- 和 34-/alphaA- 表现出胞饮作用速率降低，生长至较低的饱和密度，并在振荡培养物中产生小细胞。所有菌株在细菌悬浮液和具有菌苔的琼脂平板上正常生长。在单突变体34-和αA-以及一些双突变体菌株中分别观察到在降低温度和增加渗透压的条件下生长缓慢。 34-/alphaA-和34-/120-细胞的运动性、趋化性和发育基本没有改变。然而，34-/αA-细胞在悬浮状态下饥饿时表现出聚集增强。此外，双突变菌株的形态发生均受到损害，并且观察到形态异常的子实体。这些缺陷通过重新表达其中一种缺乏的交联蛋白而得以恢复。这些突变的附加和合成表型表明肌动蛋白交联蛋白在肌动蛋白细胞骨架中发挥着独特和重叠的功能。
The contribution of three actin cross-linking proteins, alpha-actinin (alphaA), gelation factor (ABP-120), and the 34 kDa actin-bundling protein to cellular functions has been studied in three single mutant (alphaA-, 120-, and 34-) and three double mutant (alphaA-/120-, 34-/alphaA-, 34-/120-) strains of Dictyostelium generated by homologous recombination. Strains alphaA-/120- and 34-/alphaA- exhibited a reduced rate of pinocytosis, grew to lower saturation densities, and produced small cells in shaking cultures. All strains grew normally in bacterial suspensions and on agar plates with a bacterial lawn. Slow growth under conditions of reduced temperature and increased osmolarity was observed in single mutants 34- and alphaA-, respectively, as well as in some of the double mutant strains. Motility, chemotaxis, and development were largely unaltered in 34-/alphaA- and 34-/120- cells. However, 34-/alphaA- cells showed enhanced aggregation when starved in suspension. Moreover, morphogenesis was impaired in both double mutant strains and fruiting bodies of aberrant morphology were observed. These defects were reverted by re-expression of one of the lacking cross-linking proteins. The additive and synthetic phenotypes of these mutations indicate that actin cross-linking proteins serve both unique and overlapping functions in the actin cytoskeleton.
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DOI：
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