Substructure of the outer dynein arm.
The substructure of the outer dynein arm has been analyzed in quick-frozen deep-etch replicas of Tetrahymena and Chlamydomonas axonemes. Each arm is found to be composed of five morphologically discrete components: an elliptical head; two spherical feet; a slender stalk; and an interdynein linker. The feet make contact with the A microtubule of each doublet; the stalk contacts the B microtubule; the head lies between the feet and stalk; and the linker associates each arm with its neighbor. The spatial relationships between these five components are found to be distinctly different in rigor (ATP-depleted) versus relaxed (ATP- or vanadate plus ATP-treated) axonemes, and the stalk appears to alter its affinity for the B microtubule in the relaxed state. Images of living cilia attached to Tetrahymena cells show that the relaxed configuration is adopted in vivo. We relate our observations to morphological and experimental studies reported by others and propose several models that suggest how this newly described dynein morphology may relate to dynein function.
D000251:Adenosine Triphosphatases / Q000502:physiology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002696:Chlamydomonas / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure; D002923:Cilia / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure; D004398:Dyneins / Q000502:physiology; D008854:Microscopy, Electron; D008870:Microtubules / Q000201:enzymology; D008954:Models, Biological; D008968:Molecular Conformation; D009068:Movement / Q000187:drug effects; D013768:Tetrahymena / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology
D014639:Vanadium; D014638:Vanadates; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D004398:Dyneins