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Polyglycylation domain of β-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena

Nature Cell Biology volume 4, pages 256–259 (2002)Cite this article

Abstract

Polyglycylation occurs through the post-translational addition of a polyglycine peptide to the γ-carboxyl group of glutamic acids near the C terminus of α- and β-tubulin1, and has been found only in cells with axonemes, from protists to humans2,3. In Tetrahymena thermophila, multiple sites of polyglycylation on α-tubulin are dispensable. By contrast, mutating similar sites on β-tubulin has site-specific effects, affecting cell motility and cytokinesis, or resulting in cell death4. Here, we address the lethality of a polyglycylation deficiency in T. thermophila using heterokaryons5. Cells with a lethal mutation in the polyglycylation domain of β-tubulin assembled axonemes that lack the central pair, B-subfibres and the transitional zone of outer microtubules (MTs). Furthermore, an arrest in cytokinesis occurred, and was associated with incomplete severing of cortical MTs positioned near the cleavage furrow. Thus, tubulin polyglycylation is required for the maintenance of some stable microtubular organelles that are all known to be polyglycylated in vivo, but its effects on MTs appear to be organelle-specific.

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Figure 1: Course of cytokinesis in wild-type and mutant cells.
Figure 2: Ultrastructure of wild-type and mutant cilia.
Figure 3: Immunofluorescence images of wild-type, nondividing cells.
Figure 4: Immunofluorescence images of mutant cells after phenotype induction and arrest in cytokinesis.

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Acknowledgements

This work was supported by a National Institutes of Health grant GM 54017 and an American Cancer Society grant RPG-99-245-01-CSM. We are grateful to the staff of the Center for Advanced Ultrastructural Research at the University of Georgia for training R.T. and for extensive technical assistance. We thank J. Frankel and J. Rosenbaum for numerous comments and stimulating ideas. We also thank M. Gorovsky, M. Jerka-Dziadosz, N. Williams and J. Lauderdale for critical reading of the manuscript, J. Salisbury for the 20H5 antibody, G. Piperno for the 6-11 B-1 antibody, and M.-H. Bré and N. Levilliers for the AXO49 antibodies. The 12G10 monoclonal antibody was produced by E.M. Nelsen and J. Frankel, and will be available from the Developmental Studies Hybridoma Bank developed under the auspices of the NICHD and maintained by the University of Iowa Department of Biological Sciences.

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  1. Department of Cellular Biology, University of Georgia, Athens, 30602, Georgia, USA

    Rupal Thazhath, Chengbao Liu & Jacek Gaertig

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  1. Rupal Thazhath
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  2. Chengbao Liu
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Correspondence to Jacek Gaertig.

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Thazhath, R., Liu, C. & Gaertig, J. Polyglycylation domain of β-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena. Nat Cell Biol 4, 256–259 (2002). https://doi.org/10.1038/ncb764

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