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A more recent version of this article appeared on January 1, 2003
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Submitted on May 23, 2002
Revised on August 15, 2002
Accepted on September 13, 2002
1 Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461
2 Department of Medical Biochemistry and Genetics, Panum Institute, University of Copenhagen, Denmark
* Corresponding author. E-mail address: satir{at}aecom.yu.edu.
Centrin, an EF hand Ca2+ binding protein, has been cloned in Tetrahymena thermophila. It is a 167 amino acid protein of 19.4 kDa with a unique N terminal region, coded by a single gene containing an 85 bp intron. It has > 80% homology to other centrins, and high homology to Tetrahymena EF hand proteins calmodulin and TCBP23, 25. Specific cellular localizations of the closely related Tetrahymena EF hand proteins are different from centrin. Centrin is localized to basal bodies, cortical fibers in oral apparatus and ciliary rootlets, the apical filament ring and to inner arm (14S) dynein (IAD) along the ciliary axoneme. The function of centrin in Ca2+ control of IAD activity was explored using in vitro microtubule (MT) motility assays. Ca2+ or the Ca2+ mimicking peptide CALP1 which binds EF hand proteins in the absence of Ca2+ increased MT sliding velocity. Antibodies to centrin abrogated this increase. This is the first demonstration of a specific centrin function associated with axonemal dynein. It suggests that centrin is a key regulatory protein for Tetrahymena axonemal Ca2+ responses, including ciliary reversal or chemotaxis.
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