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Originally published In Press as doi:10.1074/jbc.M210751200 on November 14, 2002

J. Biol. Chem., Vol. 278, Issue 9, 7725-7734, February 28, 2003
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Rib72, a Conserved Protein Associated with the Ribbon Compartment of Flagellar A-microtubules and Potentially Involved in the Linkage between Outer Doublet Microtubules*

Kazuho IkedaDagger §, Jennifer A. Brown§, Toshiki YagiDagger , Jan M. Norrander, Masafumi HironoDagger , Eric Eccleston||, Ritsu KamiyaDagger **, and Richard W. LinckDagger Dagger

From the Dagger  Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan and the  Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota 55455

Ciliary and flagellar axonemes are basically composed of nine outer doublet microtubules and several functional components, e.g. dynein arms, radial spokes, and interdoublet links. Each A-tubule of the doublet contains a specialized "ribbon" of three protofilaments composed of tubulin and other proteins postulated to specify the three-dimensional arrangement of the various axonemal components. The interdoublet links hold the doublet microtubules together and limit their sliding during the flagellar beat. In this study on Chlamydomonas reinhardtii, we cloned a cDNA encoding a 71,985-Da polypeptide with three DM10 repeats, two C-terminal EF-hand motifs, and homologs extending to humans. This polypeptide, designated as Rib72, is a novel component of the ribbon compartment of flagellar microtubules. It remained associated with 9-fold arrays of doublet tubules following extraction under high and low ionic conditions, and anti-Rib72 antibodies revealed an ~96-nm periodicity along axonemes, consistent with Rib72 associating with interdoublet links. Following proteolysis- and ATP-dependent disintegration of axonemes, the rate of cleavage of Rib72 correlated closely with the rate of sliding disintegration. These observations identify a ribbon-associated protein that may function in the structural assembly of the axoneme and in the mechanism and regulation of ciliary and flagellar motility.

* This work was supported by grants from the Ministry of Education, Culture, Sports, Science, and Technology of Japan and from CREST of JST (Japan Science and Technology Corporation) (to R. K.) and by United States Public Health Service Grant GM35648, National Science Foundation Research Training Group Grant DBI-9602237, University of Minnesota Grant-in-aid 17936, and Minnesota Medical Foundation Grant AO-169-00 (to R. W. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AAM44303.

§ Both authors contributed equally to this work.

|| Present address: Children's Research Inst., Children's National Medical Center, Washington D. C.

** To whom correspondence may be addressed. Tel.: 81-3-5841-4426; Fax: 81-3-5800-6842; E-mail: kamiyar@biol.s.u-tokyo.acjp.

Dagger Dagger To whom correspondence may be addressed: Dept. of Genetics, Cell Biology, and Development, 6-160 Jackson Hall, University of Minnesota, 321 Church St., Minneapolis, MN 55455. Tel.: 612-624-5179; Fax: 612-626-6140; E-mail: linck@mail.ahc.umn.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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