You can manage bookmarks using lists, please log in to your user account for this.
Media type:
E-Article
Title:
ATP Production inChlamydomonas reinhardtiiFlagella by Glycolytic Enzymes
Contributor:
Mitchell, Beth F.;
Pedersen, Lotte B.;
Feely, Michael;
Rosenbaum, Joel L.;
Mitchell, David R.
Published:
American Society for Cell Biology (ASCB), 2005
Published in:
Molecular Biology of the Cell, 16 (2005) 10, Seite 4509-4518
Language:
English
DOI:
10.1091/mbc.e05-04-0347
ISSN:
1059-1524;
1939-4586
Origination:
Footnote:
Description:
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.