Binding of Tetrahymena dynein to axonemes of Marsilea vestita lacking the outer dynein arm.
Axonemes from the heterosporous water fern Marsilea vestita were fixed in the presence of tannic acid and examined by thin-section electron microscopy. Transverse sections revealed the normal 9+2 configuration except for the absence of the outer of the two dynein arms. Both arms were normally preserved in parallel preparations of Chlamydomonas axonemes. Isolated dynein from the ciliated protozoon Tetrahymena bound to Marsilea axonemes at the site normally occupied by the outer arm. Dynein binding was partially reversed by ATP as judged by both electron microscopy and polyacrylamide gel electrophoresis. This system should provide a valuable insight into the biochemistry and function of the inner dynein arm and the relationship of the two arms to motility in more conventionally equipped axonemes.
Hyams
J S
JS
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D004398:Dyneins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008297:Male; D008854:Microscopy, Electron; D010944:Plants / Q000378:metabolism* / Q000648:ultrastructure; D013082:Sperm Tail / Q000378:metabolism*; D013094:Spermatozoa / Q000378:metabolism*; D013768:Tetrahymena / Q000378:metabolism* / Q000648:ultrastructure
D000251:Adenosine Triphosphatases; D004398:Dyneins