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MBC in Press, published online ahead of print November 24, 2004
Mol. Biol. Cell 10.1091/mbc.E04-09-0784

A more recent version of this article appeared on February 1, 2005
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Submitted on September 8, 2004
Revised on November 8, 2004
Accepted on November 11, 2004

Molecular Characterization of Radial Spoke Subcomplex Containing Radial Spoke Protein 3 and Heat Shock Protein 40 in Sperm Flagella of the Ascidian Ciona intestinalis

Yuhkoh Satouh,* Potturi Padma,* Toshifusa Toda,{dagger} Nori Satoh,{ddagger}{sect} Hiroyuki Ide,* and Kazuo Inaba*{sect}||¶

*Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences, Tohoku University, Sendai 980-8578, Japan; {dagger}TMIG Proteomics Collaboration Center, Tokyo Metropolitan Institute of Gerontology, Tokyo 173-0015, Japan; {ddagger}Department of Zoology, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan; {sect}Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Tokyo 113-0033, Japan; ||Shimoda Marine Research Center, University of Tsukuba, Shimoda 415-0025, Japan

Monitoring Editor: Paul Matsudaira

Members of the HSP40 proteins regulate the protein folding activity of HSP70 proteins and help the functional specialization of this molecular chaperone system in various types of cellular events. We have recently identified Hsp40 as a component of flagellar axoneme in the ascidian, Ciona intestinalis, suggesting a correlation between Hsp40 related chaperone system and flagellar function. In this study, we have found that Ciona 37 kDa Hsp40 is extracted from KCl-treated axonemes with 0.5 M KI solution and comigrates with radial spoke protein 3 (RSP3) along with several proteins as a complex through gel filtration and ion-exchange columns. Peptide mass fingerprinting with MALDI-TOF/MS revealed that other proteins in the complex include a homolog of sea urchin spokehead protein (homolog of RSP4/6), a MORN (membrane occupation and recognition nexus) repeat protein with sequence similarity with meichroacidin and a functionally unknown 33 kDa protein. A spoke head protein, LRR37, is not included in the complex, suggesting that the complex constructs the stalk of radial spoke. Immunoelectron microscopy indicates that Hsp40 is localized in the distal portion of spoke stalk, possibly at the junction between spoke head and the stalk.

Corresponding author. E-mail: inaba{at}kurofune.shimoda.tsukuba.ac.jp




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