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A more recent version of this article appeared on September 1, 2003
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Submitted on January 31, 2003
Revised on April 22, 2003
Accepted on April 23, 2003
1 Department of Cell Biology, University of
Massachusetts Medical School, Worcester, MA 01655, USA
2 Asamushi Marine Biological Station, Tohoku University,
Aomori 039-3501, Japan
3 Program in Molecular Medicine,
University of Massachusetts Medical School, Worcester, MA 01605, USA
4 Department of Biochemistry, University of Connecticut
Health Center, Farmington, CT 06030, USA
5 DOE Plant
Research Laboratory, Michigan State University, East Lansing, MI 48824,
USA
6 Department of Biological Sciences, Graduate School of
Science, University of Tokyo, Tokyo 113, Japan
* Corresponding author. E-mail address: george.witman{at}umassmed.edu.
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). 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 D 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 due to 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.
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