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© The Rockefeller University Press, 0021-9525/2000//1097 $5.00
The Journal of Cell Biology, Volume 149, Number 5, , 2000 1097-1106

Original Article

Polyglycylation of Tubulin Is Essential and Affects Cell Motility and Division in Tetrahymena thermophila



Lu Xiaa, Bing Haib, Yan Gaoa, Dylan Burnettea, Rupal Thazhatha, Jianming Duanb, Marie-Helene Bréc, Nicolette Levilliersc, Martin A. Gorovskyb, and Jacek Gaertiga

a Department of Cellular Biology, University of Georgia, Athens, Georgia 30602-2607
b Department of Biology, University of Rochester, Rochester, New York 14627
c Laboratoire de Biologie Cellulaire 4, CNRS UPRES-A 8080, Université Paris XI, 91405, Orsay Cedex, France
Department of Cellular Biology, 724 Biological Sciences Building, University of Georgia, Athens, GA 30602-2607.(706) 542-4271(706) 542-3409

jgaertig{at}cb.uga.edu

We analyzed the role of tubulin polyglycylation in Tetrahymena thermophila using in vivo mutagenesis and immunochemical analysis with modification-specific antibodies. Three and five polyglycylation sites were identified at glutamic acids near the COOH termini of {alpha}- and β-tubulin, respectively. Mutants lacking all polyglycylation sites on {alpha}-tubulin have normal phenotype, whereas similar sites on β-tubulin are essential. A viable mutant with three mutated sites in β-tubulin showed reduced tubulin glycylation, slow growth and motility, and defects in cytokinesis. Cells in which all five polyglycylation sites on β-tubulin were mutated were viable if they were cotransformed with an {alpha}-tubulin gene whose COOH terminus was replaced by the wild-type COOH terminus of β-tubulin. In this double mutant, β-tubulin lacked detectable polyglycylation, while the {alpha}-β tubulin chimera was hyperglycylated compared with {alpha}-tubulin in wild-type cells. Thus, the essential function of polyglycylation of the COOH terminus of β-tubulin can be transferred to {alpha}-tubulin, indicating it is the total amount of polyglycylation on both {alpha}- and β-tubulin that is essential for survival.

Key Words: motor proteins • microtubules • cilia • cytoskeleton • motility

© 2000 The Rockefeller University Press

Abbreviations used in this paper: E, glutamate residues; MT, microtubule; PTM, posttranslational modifications.


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