Parasitology Research

, Volume 94, Issue 5, pp 386–389 | Cite as

Posttranslational modifications of α-tubulin of Toxoplasma gondii

  • Uwe Plessmann
  • Ingrid Reiter-Owona
  • Karl-Ferdinand LechtreckEmail author
Short Communication


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.


Trypanosoma Glutamyl Toxoplasma Gondii Trypanosoma Brucei Glutamate Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



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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Copyright information

© Springer-Verlag 2004

Authors and Affiliations

  • Uwe Plessmann
    • 1
  • Ingrid Reiter-Owona
    • 2
  • Karl-Ferdinand Lechtreck
    • 3
    Email author
  1. 1.Department of BiochemistryMax-Planck-Institute for Biophysical ChemistryGöttingenGermany
  2. 2.Institute of Medical ParasitologyUniversity of BonnBonnGermany
  3. 3.Department of Cell Biology, R. S7-228University of Massachusetts Medical SchoolWorcesterUSA

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