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Vol. 9, Issue 12, 3335-3349, December 1998
Department of Cell Biology, Emory University School of Medicine,
Atlanta, Georgia 30322
Previous structural and biochemical studies have revealed that the
inner arm dynein I1 is targeted and anchored to a unique site located
proximal to the first radial spoke in each 96-nm axoneme repeat on
flagellar doublet microtubules. To determine whether intermediate
chains mediate the positioning and docking of dynein complexes, we
cloned and characterized the 140-kDa intermediate chain (IC140) of the
I1 complex. Sequence and secondary structural analysis, with particular
emphasis on 
-sheet organization, predicted that IC140 contains seven
WD repeats. Reexamination of other members of the dynein intermediate
chain family of WD proteins indicated that these polypeptides also bear
seven WD/-sheet repeats arranged in the same pattern along each
intermediate chain protein. A polyclonal antibody was raised against a
53-kDa fusion protein derived from the C-terminal third of IC140. The
antibody is highly specific for IC140 and does not bind to other dynein
intermediate chains or proteins in Chlamydomonas
flagella. Immunofluorescent microscopy of Chlamydomonas
cells confirmed that IC140 is distributed along the length of both
flagellar axonemes. In vitro reconstitution experiments demonstrated
that the 53-kDa C-terminal fusion protein binds specifically to
axonemes lacking the I1 complex. Chemical cross-linking indicated that
IC140 is closely associated with a second intermediate chain in the I1
complex. These data suggest that IC140 contains domains responsible for
the assembly and docking of the I1 complex to the doublet microtubule cargo.
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