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A correction to this article has been published: Kilburn et al., J. Cell Biol. 179 (1) 167
Published online September 4, 2007
doi:10.1083/jcb.200703109
The Journal of Cell Biology, Vol. 178, No. 6, 905-912
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Kilburn et al.
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New Tetrahymena basal body protein components identify basal body domain structure



Chandra L. Kilburn1, Chad G. Pearson1, Edwin P. Romijn2, Janet B. Meehl1, Thomas H. Giddings, Jr.1, Brady P. Culver1, John R. Yates, III2, and Mark Winey1

1 Molecular, Cellular, and Developmental Biology, University of Colorado at Boulder, Boulder, CO 80309
2 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037

Correspondence to Mark Winey: mark.winey{at}colorado.edu

Basal bodies organize the nine doublet microtubules found in cilia. Cilia are required for a variety of cellular functions, including motility and sensing stimuli. Understanding this biochemically complex organelle requires an inventory of the molecular components and the contribution each makes to the overall structure. We define a basal body proteome and determine the specific localization of basal body components in the ciliated protozoan Tetrahymena thermophila. Using a biochemical, bioinformatic, and genetic approach, we identify 97 known and candidate basal body proteins. 24 novel T. thermophila basal body proteins were identified, 19 of which were localized to the ultrastructural level, as seen by immunoelectron microscopy. Importantly, we find proteins from several structural domains within the basal body, allowing us to reveal how each component contributes to the overall organization. Thus, we present a high resolution localization map of basal body structure highlighting important new components for future functional studies.

C.L. Kilburn and C.G. Pearson contributed equally to this paper.

E.P. Romijn's present address is Philips Research, 5656AA Eindhoven, Netherlands.

Abbreviations used in this paper: HB, homogenization buffer; IB, isolation buffer; MudPIT, multidimensional protein identification technology; SPP, super proteose peptone.


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