Journal of Biochemistry Advance Access published online on August 26, 2006
Journal of Biochemistry, doi:10.1093/jb/mvj182
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1 Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan; Present address: Research Institute for Cell Engineering, National Institute for Advanced Industrial Science and Technology, Tsukuba Central 4, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8562, Japan
* To whom correspondence should be addressed. 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+/CaM-associated 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 don't 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.
Received July 11, 2006
Accepted August 22, 2006
Regular Paper
Homologues of Radial Spoke Head Proteins Interact with Ca2+/Calmodulin in Tetrahymena Cilia
Hironori Ueno 1, Yoshinori Iwataki 2, and Osamu Numata 2 *
2 Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan
Osamu Numata, E-mail: numata{at}sakura.cc.tsukuba.ac.jp
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