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Eukaryotic Cell, February 2004, p. 212-220, Vol. 3, No. 1
1535-9778/04/$08.00+0 DOI: 10.1128/EC.3.1.212-220.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
- and ß-Tubulins
Centre de Génétique Moléculaire, CNRS, 91198 Gif-sur-Yvette,1 Ecole Supérieure de Physique et Chimie Industrielles, 75005 Paris,2 Institut de Biologie Moléculaire des Plantes, CNRS, 67083 Strasbourg Cedex, France3
Received 3 October 2003/ Accepted 12 December 2003
The thermosensitive allelic mutations sm19-1 and sm19-2 of Paramecium tetraurelia cause defective basal body duplication: growth at the nonpermissive temperature yields smaller and smaller cells with fewer and fewer basal bodies. Complementation cloning of the SM19 gene identified a new tubulin, eta-tubulin, showing low homology with each of the other five tubulins,
to
, characterized in P. tetraurelia. In order to analyze
-tubulin functions, we used a genetic approach to identify interacting molecules. Among a series of extragenic suppressors of the sm19-1 mutation, the su3-1 mutation was characterized as an E288K substitution in the ß-PT2 gene coding for a ß-tubulin, while the mutation nocr1 conferring nocodazole resistance and localized in another ß-tubulin gene, ß-PT3, was shown to enhance the mutant phenotype. The interaction between
-tubulin and microtubules, revealed by genetic data, is supported by two further types of evidence: first, the mutant phenotype is rescued by taxol, which stabilizes microtubules; second, molecular modeling suggests that
-tubulin, like
- and
-tubulins, might be a microtubule minus-end capping molecule. The likely function of
-tubulin as part of a complex specifically involved in basal body biogenesis is discussed.
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