The outer dynein arm-docking complex: composition and characterization of a subunit (oda1) necessary for outer arm assembly
UMass Chan Affiliations
Department of Cell BiologyDocument Type
Journal ArticlePublication Date
2002-03-22Keywords
Algal ProteinsAmino 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
Metadata
Show full item recordAbstract
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.Source
Mol Biol Cell. 2002 Mar;13(3):1015-29. Link to article on publisher's siteDOI
10.1091/mbc.01-04-0201Permanent Link to this Item
http://hdl.handle.net/20.500.14038/38521PubMed ID
11907279Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1091/mbc.01-04-0201