Skip Navigation


Journal of Biochemistry Advance Access originally published online on August 26, 2006
Journal of Biochemistry 2006 140(4):525-533; doi:10.1093/jb/mvj182
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
140/4/525    most recent
mvj182v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Ueno, H.
Right arrow Articles by Numata, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ueno, H.
Right arrow Articles by Numata, O.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

ARTICLE

Homologues of Radial Spoke Head Proteins Interact with Ca2+/Calmodulin in Tetrahymena Cilia

Hironori Ueno*, Yoshinori Iwataki and Osamu Numata{dagger}

Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8572

{dagger} To whom correspondence should be addressed. Tel: +81-29-853-6648, Fax: +81-29-853-6614, E-mail numata{at}sakura.cc.tsukuba.ac.jp

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 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.

* 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.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.