The Journal of Cell Biology, Vol 105, 897-901, Copyright © 1987 by The Rockefeller University Press
Chymotryptic digestion of Tetrahymena ciliary dynein. II. Pathway of the degradation of 22S dynein heavy chains
YY Toyoshima
As shown in the preceding paper (Toyoshima, Y. Y., 1987, J. Cell Biol.,
105:887-895) three-headed Tetrahymena 22S dynein consists of three heavy
chains (HCs) and is decomposed into two-headed (H) and one-headed (L)
fragments by chymotryptic digestion. To accurately determine the presence
of multiple ATPases and ultimately the location of various domains, it is
necessary to determine the identity of each HC fragment relative to the
original HCs in 22S dynein. The degradation pathway of each HC was
determined by peptide mapping and immunoblotting. The three HCs (A alpha, A
beta, and A gamma) were immunologically different; although SDS-urea gel
electrophoresis showed that A gamma HC was apparently resistant to the
digestion, actually three distinct HCs contributed to the same band
alternately. H fragment was derived from A beta and A gamma HCs, whereas L
fragment originated from A alpha HC. Since both fragments were associated
with ATPase activity, these results directly demonstrate the presence of
multiple ATPase sites in Tetrahymena 22S dynein.
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