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

Reverse-transcriptase polymerase chain reaction cloning of the 3'-ends of the alpha-tubulin cDNAs of Tritrichomonas mobilensis in combination with Southern-blot analysis identified seven to eight distinct alpha-tubulin genes. All seven lack a carboxy-terminal tyrosine and the corresponding sequence compatible with posttranslational tyrosination. This indicates that whereas tyrosination of alpha-tubulin has been found in most species, including humans and trypanosomes, it is absent in trichomonads.