ATP Production in Chlamydomonas reinhardtii Flagella by Glycolytic Enzymes

TY - JOUR

T1 - ATP Production in Chlamydomonas reinhardtii Flagella by Glycolytic Enzymes

AU - Mitchell, Beth F

AU - Pedersen, Lotte B

AU - Feely, Michael

AU - Rosenbaum, Joel L

AU - Mitchell, David R

N1 - Keywords: Adenosine Triphosphate; Amino Acid Sequence; Animals; Chlamydomonas reinhardtii; Cilia; Flagella; Microscopy, Electron, Transmission; Molecular Sequence Data; Phosphoglycerate Mutase; Phosphopyruvate Hydratase; Protein Subunits; Pyruvate Kinase

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

U2 - 10.1091/mbc.E05-04-0347

DO - 10.1091/mbc.E05-04-0347

M3 - Journal article

C2 - 16030251

SN - 1059-1524

VL - 16

SP - 4509

EP - 4518

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

IS - 10

ER -