CHE-3, a cytosolic dynein heavy chain, is required for sensory cilia structure and function in Caenorhabditis elegans
CHE-3, a cytosolic dynein heavy chain, is required for sensory cilia structure and function in Caenorhabditis elegans
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DOI：
10.1006/dbio.2000.9686
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发表时间：
2000-05-15
影响因子：
2.7
通讯作者：
Plasterk, RHA
中科院分区：
文献类型：
--
作者：
Wicks, SR;de Vries, CJ;Plasterk, RHA
利用线虫对可溶性化合物趋化性的新方法进行正向遗传筛选，在编码秀丽隐杆线虫动力蛋白重链（DHC） 1b亚型的基因中发现了三个独立的转座子插入突变。使用新开发的基于pcr的转座子显示对这些中断进行了映射和克隆。这些突变被证明是che-3基因座的等位基因。这种动力蛋白同工型在纤毛感觉神经元中表现出时间和空间上的限制性表达，突变体表现出化学感觉纤毛的进行性发育缺陷。这些结果与该运动蛋白在鞭毛内运输过程中的作用一致；DHC 1b与许多其他蛋白质协同作用，以建立和维持秀丽隐杆线虫纤毛感觉末梢的结构完整性。(C) 2000年学术出版社。
Forward genetic screens using novel assays of nematode chemotaxis to soluble compounds identified three independent transposon-insertion mutations in the gene encoding the Caenorhabditis elegans dynein heavy chain (DHC) 1b isoform. These disruptions were mapped and cloned using a newly developed PCR-based transposon display. The mutations were demonstrated to be allelic to the che-3 genetic locus. This isoform of dynein shows temporally and spatially restricted expression in ciliated sensory neurons, and mutants show progressive developmental defects of the chemosensory cilia. These results are consistent with a role for this motor protein in the process of intraflagellar transport; DHC 1b acts in concert with a number of other proteins to establish and maintain the structural integrity of the ciliated sensory endings in C. elegans. (C) 2000 Academic Press.