An actin point-mutation neighboring the 'hydrophobic plug' causes defects in the maintenance of cell polarity and septum organization in the fission yeast Schizosaccharomyces pombe
An actin point-mutation neighboring the 'hydrophobic plug' causes defects in the maintenance of cell polarity and septum organization in the fission yeast Schizosaccharomyces pombe
复制标题
DOI：
10.1016/0014-5793(96)00819-8
复制
发表时间：
1996-09-02
期刊：
影响因子：
3.5
通讯作者：
Kobayashi, W
中科院分区：
文献类型：
--
作者：
Ishiguro, J;Kobayashi, W
裂殖酵母cps 8突变引起异常扩大和dispolarized细胞，其中每一个包含几个细胞核与异常的多隔膜。分子克隆和序列分析表明，cps 8基因编码的肌动蛋白与氨基酸取代的天冬氨酸甘氨酸残基273在疏水环，位于肌动蛋白亚结构域3和4之间。使用鬼笔环肽和抗肌动蛋白抗体的荧光显微镜显示突变细胞中的F-肌动蛋白结构和分布的变化。这些结果表明，疏水环在形成正常的F-肌动蛋白结构中起着至关重要的作用，只有这样，细胞极性和晚期有丝分裂事件才能得到适当的维持。
The fission yeast cps8 mutation gives rise to abnormally enlarged and dispolarized cells, each of which contains several nuclei with aberrant multisepta. Molecular cloning and sequence analysis of the cps8 gene indicated that it encodes an actin with an amino acid substitution of aspartic acid for glycine at residue 273 in the hydrophobic loop that is located between actin subdomains 3 and 4. Fluorescence microscopy using phalloidin and anti-actin antibody revealed changes in the F-actin structure and distribution in the mutant cells. These results indicate that the hydrophobic loop plays an essential role for creating normal F-actin structure, only by which cell polarity and the late mitotic events can be maintained properly.