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Vol. 14, Issue 9, 3650-3663, September 2003
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* Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655;
Asamushi Marine Biological Station, Tohoku University, Aomori 039-3501, Japan;
Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605;
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030;
¶ DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824; and
|| Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113, Japan
Submitted January 31, 2003;
Revised April 22, 2003;
Accepted April 23, 2003
Monitoring Editor: Paul Matsudaira
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.
Abbreviations used: BAC, bacterial artificial chromosome; EM, electron microscopy; EV, ExpertVision; HRP, horseradish peroxidase; IC, dynein intermediate chain; LC, dynein light chain; ODA-DC, outer dynein arm-docking complex; PCR, polymerase chain reaction; PVDF, polyvinylidene difluoride; RFLP, restriction fragment length polymorphism.
# Corresponding author. E-mail address: george.witman{at}umassmed.edu.
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