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Vol. 13, Issue 3, 1015-1029, March 2002
and
*Department of Cell Biology, University of Massachusetts Medical
School, Worcester, Massachusetts 01655; 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. 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-kDa protein with potential homologs 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.
Department of
Biological Sciences, Graduate School of Science, University of Tokyo,
Tokyo 113, Japan; and National Institute for Basic
Biology, Okazaki 444-8585, Japan
Program in Molecular Medicine,
University of Massachusetts Medical School, Worcester, MA 01605;
§Michigan State University-Department of Energy Plant
Research Laboratory, East Lansing, MI 48824.
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