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MBC in Press, published online ahead of print February 20, 2004
Mol. Biol. Cell 10.1091/mbc.E03-11-0854

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Submitted on November 28, 2003
Revised on January 27, 2004
Accepted on January 27, 2004

A Tektin Homologue Is Decreased in Chlamydomonas Mutants Lacking an Axonemal Inner-Arm Dynein

Haru-aki Yanagisawa1 and Ritsu Kamiya1*

1 Department of Biological Sciences, Graduate School of Science, University of Tokyo, and CREST, Japan Science and Technology Corporation

* Corresponding author. E-mail address: kamiyar{at}biol.s.u-tokyo.ac.jp.

In ciliary and flagellar axonemes, various discrete structures such as inner and outer dynein arms are regularly arranged on the outer doublet microtubules. Little is known about the basis for their regular arrangement. In this study, proteins involved in the attachment of inner-arm dyneins were searched by a microtubule overlay assay on Chlamydomonas mutant axonemes. A 58-kDa protein (p58) was found ~80% diminished in the mutants ida6 and pf3, both lacking one (species e) of the seven inner arm species (a-g). Analysis of its cDNA indicated that p58 is homologous to tektin, a protein that was originally found in sea urchin and thought to be crucial for the longitudinal periodicity of the doublet microtubule. Unlike sea urchin tektin, which is a component of protofilament ribbons that appear after Sarkosyl treatment of axonemes, p58 was not contained in similar Sarkosyl-resistant ribbons from Chlamydomonas axonemes. Immunofluorescence microscopy showed that p58 was localized uniformly along the axoneme and on the basal body. The p58 signal was reduced in ida6 and pf3. These results suggest that a reduced amount of p58 is sufficient for the production of outer doublets, while an additional amount of it is involved in inner-arm dynein attachment.




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