Yamamoto Ryosuke, Yanagisawa Haru-aki, Yagi Toshiki, Kamiya Ritsu
Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Tokyo 113-0033, Japan.
FEBS Lett. 2006 Nov 27;580(27):6357-60. doi: 10.1016/j.febslet.2006.10.047. Epub 2006 Nov 10.
To elucidate the subunit composition of axonemal inner-arm dynein, we examined a 38 kDa protein (p38) co-purified with a Chlamydomonas inner arm subspecies, dynein d. We found it is a novel protein conserved among a variety of organisms with motile cilia and flagella. Immunoprecipitation using specific antibody verified its association with a heavy chain, actin and a previously identified light chain (p28). Unexpectedly, mutant axonemes lacking dynein d and other dyneins retained reduced amounts of p38. This finding suggests that p38 is involved in the docking of dynein d to specific loci.
为阐明轴丝内臂动力蛋白的亚基组成，我们检测了一种与衣藻内臂亚种动力蛋白d共纯化的38 kDa蛋白（p38）。我们发现它是一种在多种具有活动纤毛和鞭毛的生物体中保守的新型蛋白。使用特异性抗体进行免疫沉淀证实了它与一条重链、肌动蛋白和先前鉴定的一条轻链（p28）的关联。出乎意料的是，缺乏动力蛋白d和其他动力蛋白的突变轴丝保留了少量的p38。这一发现表明p38参与动力蛋白d与特定位点的对接。
