title: Posttranslational modifications of alpha-tubulin of Toxoplasma gondii.
abstract: 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.
authors.affiliation: Department of Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Uwe
authors.initials: U
authors.lastname: Plessmann
authors.forename: Ingrid
authors.initials: I
authors.lastname: Reiter-Owona
authors.forename: Karl-Ferdinand
authors.initials: KF
authors.lastname: Lechtreck
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D017422:Sequence Analysis, DNA; D014122:Toxoplasma / Q000378:metabolism*; D014404:Tubulin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D014404:Tubulin