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Vol. 16, Issue 8, 3606-3619, August 2005
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* Department of Molecular, Cellular, and Developmental Biology, University of Colorado–Boulder, Boulder, CO 80309;
Department of Biology, Colgate University, Hamilton, NY 13346
Submitted October 22, 2004;
Revised April 27, 2005;
Accepted May 31, 2005
Monitoring Editor: Joseph Gall
Centrins, small calcium binding EF-hand proteins, function in the duplication of a variety of microtubule organizing centers. These include centrioles in humans, basal bodies in green algae, and spindle pole bodies in yeast. The ciliate Tetrahymena thermophila contains at least four centrin genes as determined by sequence homology, and these have distinct localization and expression patterns. CEN1's role at the basal body was examined more closely. The Cen1 protein localizes primarily to two locations: one is the site at the base of the basal body where duplication is initiated. The other is the transition zone between the basal body and axoneme. CEN1 is an essential gene, the deletion of which results in the loss of basal bodies, which is likely due to defects in both basal body duplication and basal body maintenance. Analysis of the three other centrins indicates that two of them function at microtubule-rich structures unique to ciliates, whereas the fourth is not expressed under conditions examined in this study, although when artificially expressed it localizes to basal bodies. This study provides evidence that in addition to its previously known function in the duplication of basal bodies, centrin is also important for the integrity of these organelles.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Present address: Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia
Present address: SUNY Upstate Medical University, 750 East Adams St., Syracuse, NY 13210-2375
|| Present address: The American Association for the Advancement of Science, 1200 New York Ave. NW, Washington, DC 20005.
Address correspondence to: Mark Winey (mark.winey{at}colorado.edu).
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