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    DC3, the 21-kDa subunit of the outer dynein arm-docking complex (ODA-DC), is a novel EF-hand protein important for assembly of both the outer arm and the ODA-DC

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    Authors
    Casey, Diane M.
    Inaba, Kazuo
    Pazour, Gregory J.
    Takada, Saeko
    Wakabayashi, Ken-ichi
    Wilkerson, Curtis G.
    Kamiya, Ritsu
    Witman, George B.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Department of Cell Biology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2003-09-16
    Keywords
    Amino Acid Sequence; Animals; Cell Movement; Chlamydomonas reinhardtii; Cloning, Molecular; Dynein ATPase; Flagella; Microscopy, Electron; Microtubules; Models, Molecular; Molecular Sequence Data; Mutation; Phylogeny; Protein Subunits; Protozoan Proteins; Sequence Alignment
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1091/mbc.E03-01-0057
    Abstract
    The outer dynein arm-docking complex (ODA-DC) is a microtubule-associated structure that targets the outer dynein arm to its binding site on the flagellar axoneme (Takada et al. 2002. Mol. Biol. Cell 13, 1015-1029). The ODA-DC of Chlamydomonas contains three proteins, referred to as DC1, DC2, and DC3. We here report the isolation and sequencing of genomic and full-length cDNA clones encoding DC3. The sequence predicts a 21,341 Da protein with four EF-hands that is a member of the CTER (calmodulin, troponin C, essential and regulatory myosin light chains) group and is most closely related to a predicted protein from Plasmodium. The DC3 gene, termed ODA14, is intronless. Chlamydomonas mutants that lack DC3 exhibit slow, jerky swimming because of loss of some but not all outer dynein arms. Some outer doublet microtubules without arms had a "partial" docking complex, indicating that DC1 and DC2 can assemble in the absence of DC3. In contrast, DC3 cannot assemble in the absence of DC1 or DC2. Transformation of a DC3-deletion strain with the wild-type DC3 gene rescued both the motility phenotype and the structural defect, whereas a mutated DC3 gene was incompetent to rescue. The results indicate that DC3 is important for both outer arm and ODA-DC assembly.
    Source
    Mol Biol Cell. 2003 Sep;14(9):3650-63. Epub 2003 Jun 27. Link to article on publisher's site
    DOI
    10.1091/mbc.E03-01-0057
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/33333
    PubMed ID
    12972554
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1091/mbc.E03-01-0057
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    Morningside GSBS Scholarly Publications
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