Department of Cell Biology
Algal Proteins; Amino Acid Sequence; Animals; Base Sequence; Chlamydomonas; Dynein ATPase; Flagella; Humans; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Molecular Weight; Peptides; Protein Structure, Secondary; Protein Subunits; Protozoan Proteins; Sequence Alignment
Life Sciences | Medicine and Health Sciences
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 M(r) approximately 105,000 and approximately 70,000 proteins plus a third protein of M(r) approximately 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 M(r) approximately 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 M(r) approximately 70,000 protein. These results demonstrate that the ODA1 gene encodes the M(r) approximately 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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Citation: Mol Biol Cell. 2002 Mar;13(3):1015-29. Link to article on publisher's site
Takada, Saeko; Wilkerson, Curtis G.; Wakabayashi, Ken-ichi; Kamiya, Ritsu; and Witman, George B., "The outer dynein arm-docking complex: composition and characterization of a subunit (oda1) necessary for outer arm assembly" (2002). Open Access Articles. Paper 1393.