Recombination of ciliary dynein of Tetrahymena with the outer fibers.
Recombination of ciliary dyneins of Tetrahymena pyriformis with the outer fibers was investigated using turbidimetry, co-sedimentation analysis and electron microscopy. As reported by Gibbons, 30S dynein could recombine with the outer fibers, while 14S dynein did to so a lesser extent. At acidic pH, however, most of the 14S dynein was also rebound to the outer fibers. When an excess of crude dynein fraction was added to the outer fiber fraction at pH 8.2, electron microscopic observations showed that the outer doublet microtubules were decorated not only with arms but also with other electron-dense materials. On the other hand, when crude dynein fraction was mixed with the outer fibers in an appropriate quantity, only arms were reconstituted at the regular positions of A-subfibers. ATP had an inhibitory effect on the recombination of dynein with the outer fibers.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000494:pharmacology; D002923:Cilia / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D005407:Flagella / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008870:Microtubules / Q000201:enzymology / Q000378:metabolism / Q000648:ultrastructure; D009391:Nephelometry and Turbidimetry; D013768:Tetrahymena / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure
D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D008274:Magnesium