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J. Cell Biol.,
Volume 144, Number 2, January 25, 1999 293-304
* Department of Anatomy and Cell Biology, State University of New York Health Science Center, Syracuse, New York 13210;
and Two alleles at a new locus, central pair-associated complex 1 (CPC1), were selected in a screen for
Chlamydomonas flagellar motility mutations. These
mutations disrupt structures associated with central
pair microtubules and reduce flagellar beat frequency, but do not prevent changes in flagellar activity associated with either photophobic responses or phototactic
accumulation of live cells. Comparison of cpc1 and pf6
axonemes shows that cpc1 affects a row of projections
along C1 microtubules distinct from those missing in
pf6, and a row of thin fibers that form an arc between the two central pair microtubules. Electron microscopic
images of the central pair in axonemes from radial
spoke-defective strains reveal previously undescribed
central pair structures, including projections extending
laterally toward radial spoke heads, and a diagonal link
between the C2 microtubule and the cpc1 projection. By SDS-PAGE, cpc1 axonemes show reductions of
350-, 265-, and 79-kD proteins. When extracted from
wild-type axonemes, these three proteins cosediment
on sucrose gradients with three other central pair proteins (135, 125, and 56 kD) in a 16S complex. Characterization of cpc1 provides new insights into the structure and biochemistry of the central pair apparatus, and
into its function as a regulator of dynein-based motility.
Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322
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