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Research Article |
-tubulin at microtubule nucleation sites and is required for microtubule nucleation

1 Institut de Biologie Moléculaire des Plantes, Centre National de la
Recherche Scientifique UPR 2357, Université Louis Pasteur, 12 rue du
Général Zimmer F-67084, Strasbourg Cedex, France
2 Institut für Allgemeine Botanik, Hamburg, Ohnhorststr. 18, D-22609
Hamburg, Germany
* Present address: Laboratoire de Physiologie Cellulaire Végétale,
UMR 5019 CEA/CNRS/UJF, CEA Grenoble, 17 Avenue des Martyrs 38054 Grenoble
cedex 9, France
Author for correspondence (e-mail:
anne-catherine.schmit{at}ibmp-ulp.u-strasbg.fr
)
Accepted 13 March 2002
The molecular basis of microtubule nucleation is still not known in higher
plant cells. This process is better understood in yeast and animals cells. In
the yeast spindle pole body and the centrosome in animal cells,
-tubulin small complexes and
-tubulin ring complexes,
respectively, nucleate all microtubules. In addition to
-tubulin,
Spc98p or its homologues plays an essential role. We report here the
characterization of rice and Arabidopsis homologues of
SPC98. Spc98p colocalizes with
-tubulin at the nuclear surface
where microtubules are nucleated on isolated tobacco nuclei and in living
cells. AtSpc98p-GFP also localizes at the cell cortex. Spc98p is not
associated with
-tubulin along microtubules. These data suggest that
multiple microtubule-nucleating sites are active in plant cells. Microtubule
nucleation involving Spc98p-containing
-tubulin complexes could then be
conserved among all eukaryotes, despite differences in structure and spatial
distribution of microtubule organizing centers.
Key words:
-TuSCs,
-TuRCs, Arabidopsis, Tobacco BY-2 cells
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