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Vol. 16, Issue 10, 4509-4518, October 2005

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ATP Production in Chlamydomonas reinhardtii Flagella by Glycolytic Enzymes

Beth F. Mitchell ^*, Lotte B. Pedersen , Michael Feely ^*, Joel L. Rosenbaum , and David R. Mitchell 

^* Department of Biology, Le Moyne College, Syracuse, NY 13210; Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520; and Department of Cell and Developmental Biology, SUNY Upstate Medical University, Syracuse, NY 13210

Submitted April 25, 2005; Revised July 6, 2005; Accepted July 12, 2005
Monitoring Editor: J. Richard McIntosh

Eukaryotic cilia and flagella are long, thin organelles, and diffusion from the cytoplasm may not be able to support the high ATP concentrations needed for dynein motor activity. We discovered enzyme activities in the Chlamydomonas reinhardtii flagellum that catalyze three steps of the lower half of glycolysis (phosphoglycerate mutase, enolase, and pyruvate kinase). These enzymes can generate one ATP molecule for every substrate molecule consumed. Flagellar fractionation shows that enolase is at least partially associated with the axoneme, whereas phosphoglycerate mutase and pyruvate kinase primarily reside in the detergent-soluble (membrane + matrix) compartments. We further show that axonemal enolase is a subunit of the CPC1 central pair complex and that reduced flagellar enolase levels in the cpc1 mutant correlate with the reduced flagellar ATP concentrations and reduced in vivo beat frequencies reported previously in the cpc1 strain. We conclude that in situ ATP synthesis throughout the flagellar compartment is essential for normal flagellar motility.

Abbreviations used: GAP, glyceraldehyde 3-phosphate dehydrogenase; IFT, intraflagellar transport.

Address correspondence to: David R. Mitchell (mitcheld{at}upstate.edu).

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