期刊
JOURNAL OF BIOCHEMISTRY
卷 140, 期 4, 页码 525-533出版社
JAPANESE BIOCHEMICAL SOC
DOI: 10.1093/jb/mvj182
关键词
calcium; calmodulin; cilia; flagella; radial spoke head; Tetrahymena
Calmodulin (CaM) is an axonemal component. To examine the pathway of Ca2+/CaM signaling in cilia, using Ca2+/CaM-affinity column, we identified seven Ca2+/CaMassociated proteins from a crude dynein fraction and isolated 62 kDa (p62) and 66 kDa (P66) Ca2+/CaM-associated proteins in Tetrahymena cilia. The amino acid sequences deduced from the p62 and p66 cDNA sequences suggested that these proteins were similar to Chlamydomonas radial spoke proteins 4 and 6 (RSP4 and RSP6), components of the radial spoke head, and sea urchin sperm p63, which is a homologue of RSP4/6, and isolated as a key component that affect flagellar bending patterns. Although p62 and p66 do not have a conventional CaM-binding site, those have consecutive sequences which showed high normalized scores (>= 5) from a CaM target database. These consecutive sequences were also found in RSP4, RSP6, and p63. These radial spoke heads proteins have a high similarity region composed of 15 amino acids between the five proteins. Immunoelectron microscopy using anti-CaM antibody showed that CaM was localized along the outer edge of the curved central pair microtubules in axoneme. Therefore, it is possible that the interaction between Ca2+/CaM and radial spoke head control axonemal curvature in the ciliary and flagellar waveform.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据