Novel 44-Kilodalton Subunit of Axonemal Dynein Conserved from Chlamydomonas to Mammals
Novel 44-Kilodalton Subunit of Axonemal Dynein Conserved from Chlamydomonas to Mammals
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DOI：
10.1128/ec.00341-07
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发表时间：
2007-11
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影响因子：
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通讯作者：
Ryosuke Yamamoto;Haruaki Yanagisawa;T. Yagi;R. Kamiya
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作者：
Ryosuke Yamamoto;Haruaki Yanagisawa;T. Yagi;R. Kamiya
纤毛和鞭毛的内臂和外臂上都含有多种动力蛋白。衣原体内臂动力蛋白至少包含7个主要亚种（动力蛋白a至动力蛋白g），其中除了动力蛋白f（也称为动力蛋白I1）外，其他均为单头型，由单个重链、肌动蛋白和中心蛋白或28 kDa蛋白（p28）组成。发现动力蛋白d与另外两种38 kDa（p38）和44 kDa（p44）的蛋白质结合。在对p38蛋白（R. Yamamoto，H. A.柳泽T. Yagi和R. Kamiya，FEBS Lett. 580：6357-6360，2006），我们已经通过使用免疫沉淀方法将p44鉴定为动力蛋白D的新组分。p44沿着轴丝的长度存在，并且在IDA 4和IDA 5突变体中减少，但不是不存在，这两种突变体都缺乏这种动力蛋白。在ida 5轴丝中，p44和p38似乎形成复合物，这表明它们构成了动力蛋白d在外部双联体上的对接位点。p44在其他纤毛生物中具有潜在的同源物。例如，发现p44的小鼠同源物NYD-SP14在具有运动纤毛和鞭毛的组织中强烈表达。这些结果表明，内臂动力蛋白d及其亚基组织是广泛保守的。
ABSTRACT Cilia and flagella have multiple dyneins in their inner and outer arms. Chlamydomonas inner-arm dynein contains at least seven major subspecies (dynein a to dynein g), of which all but dynein f (also called dynein I1) are the single-headed type that are composed of a single heavy chain, actin, and either centrin or a 28-kDa protein (p28). Dynein d was found to associate with two additional proteins of 38 kDa (p38) and 44 kDa (p44). Following the characterization of the p38 protein (R. Yamamoto, H. A. Yanagisawa, T. Yagi, and R. Kamiya, FEBS Lett. 580:6357-6360, 2006), we have identified p44 as a novel component of dynein d by using an immunoprecipitation approach. p44 is present along the length of the axonemes and is diminished, but not absent, in the ida4 and ida5 mutants, both lacking this dynein. In the ida5 axoneme, p44 and p38 appear to form a complex, suggesting that they constitute the docking site of dynein d on the outer doublet. p44 has potential homologues in other ciliated organisms. For example, the mouse homologue of p44, NYD-SP14, was found to be strongly expressed in tissues with motile cilia and flagella. These results suggest that inner-arm dynein d and its subunit organization are widely conserved.