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A more recent version of this article appeared on March 1, 2002
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Submitted on April 25, 2001
Revised on November 16, 2001
Accepted on December 24, 2001
1 Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, and Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113, Japan (present address: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605)
2 Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655 (present address: Michigan State University, Department of Energy Plant Research Laboratory, East Lansing, MI 48824)
3 Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113, Japan, and National Institute for Basic Biology, Okazaki, Japan
4 Department of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655
* Corresponding author. E-mail address: George.Witman{at}umassmed.edu.
To learn more about how dyneins are targeted to specific sites in the flagellum, we have investigated a factor necessary for binding of outer arm dynein to the axonemal microtubules of Chlamydomonas. This factor, termed the outer dynein arm-docking complex (ODA-DC), previously was shown to be missing from axonemes of the outer dynein armless mutants oda1 and oda3 (Takada and Kamiya, 1994. J. Cell Biol. 126:737-745). We have now partially purified the ODA-DC, determined that it contains equimolar amounts of Mr ~105,000 and ~70,000 proteins plus a third protein of Mr ~25,000, and found that it is associated with the isolated outer arm in a 1:1 molar ratio. We have cloned a full-length cDNA encoding the Mr ~70,000 protein; the sequence predicts a 62.5-kD protein with potential homologues in higher ciliated organisms, including humans. Sequencing of corresponding cDNA from strain oda1 revealed it has a mutation resulting in a stop codon just downstream of the initiator ATG; thus it is unable to make the full-length Mr ~70,000 protein. These results demonstrate that the ODA1 gene encodes the Mr ~70,000 protein, and that the protein is essential for assembly of the ODA-DC and the outer dynein arm onto the doublet microtubule.
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