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Posttranslational modifications of α-tubulin of Toxoplasma gondii

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Abstract

The posttranslational modifications of α-tubulin of Toxoplasma gondii were characterized by antibodies and biochemical analysis of the carboxy-terminal peptide. α-Tubulin is acetylated and glutamylated. Side chains with up to three glutamate residues are linked to Glu445 of T. gondii α-tubulin. The data suggest that the site of glutamylation on α-tubulin is conserved over a broad range of species.

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Acknowledgements

We thank Bernard Eddé (Montpellier, France), Philippe Huitorel (Villefranche-sur-mer, France), and Joel Rosenbaum (New Haven, USA) for antibody gifts and Klaus Weber (Göttingen) for support and discussion. The experiments comply with the laws of Germany. This study was supported by the Deutsche Forschungsgemeinschaft (DFG).

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Authors and Affiliations

  1. Department of Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany

    Uwe Plessmann

  2. Institute of Medical Parasitology, University of Bonn, Bonn, Germany

    Ingrid Reiter-Owona

  3. Department of Cell Biology, R. S7-228, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA

    Karl-Ferdinand Lechtreck

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  1. Uwe Plessmann
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  2. Ingrid Reiter-Owona
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  3. Karl-Ferdinand Lechtreck
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Correspondence to Karl-Ferdinand Lechtreck.

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Plessmann, U., Reiter-Owona, I. & Lechtreck, KF. Posttranslational modifications of α-tubulin of Toxoplasma gondii. Parasitol Res 94, 386–389 (2004). https://doi.org/10.1007/s00436-004-1220-7

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  • DOI: https://doi.org/10.1007/s00436-004-1220-7

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