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© The Rockefeller University Press, 0021-9525/1999//293 $5.00
The Journal of Cell Biology, Volume 144, Number 2, , 1999 293-304

Regular Articles

Characterization of a Chlamydomonas Insertional Mutant that Disrupts Flagellar Central Pair Microtubule-associated Structures



David R. Mitchell* and Winfield S. Sale{ddagger}

* Department of Anatomy and Cell Biology, State University of New York Health Science Center, Syracuse, New York 13210; and {ddagger} Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322

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.

Key Words: cilia • flagella • motility • microtubule • Chlamydomonas

Address correspondence to David R. Mitchell, Department of Anatomy, SUNY Health Science Center, 750 E. Adams Street, Syracuse, NY 13210. Tel.: (315) 464-8575. Fax: (315) 464-8535. E-mail: mitcheld{at}vax.cs.hscsyr.edu

D. Mitchell would like to express his appreciation to all members of the Sale lab, where most of this work was done, and acknowledge contributions from Kim Brown (plasmid rescue and Southern blotting). We would also like to thank M. Bernstein for provided anti-Klp1 antibodies, and Eileen O'Toole for the image averaging.


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