The outer dynein arm-docking complex: Composition and characterization of a subunit (Oda1) necessary for outer arm assembly
Autor: | Ritsu Kamiya, Ken-ichi Wakabayashi, George B. Witman, Saeko Takada, Curtis G. Wilkerson |
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Rok vydání: | 2002 |
Předmět: |
Models
Molecular Macromolecular Substances Protein subunit Molecular Sequence Data Dynein Protozoan Proteins Flagellum Article Protein Structure Secondary Protein structure Microtubule Complementary DNA Animals Humans Amino Acid Sequence Molecular Biology Base Sequence biology Algal Proteins Chlamydomonas Dyneins Cell Biology biology.organism_classification Molecular biology Molecular Weight Protein Subunits Flagella Outer dynein arm Peptides Sequence Alignment |
Zdroj: | Molecular Biology of the Cell. 13:1015-1029 |
ISSN: | 1939-4586 1059-1524 |
DOI: | 10.1091/mbc.01-04-0201 |
Popis: | 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 ofChlamydomonas. 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 ofMr∼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 theMr∼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. |
Databáze: | OpenAIRE |
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