Posttranslational modifications of α‐ and β‐tubulin in Giardia lamblia, an ancient eukaryote

FEBS Letters

Schneider, André²  Weber, Klaus¹  Westermann, Stefan¹  Müller, Norbert³  Plessmann, Uwe¹ 

[1] Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Am Fassberg 11, D-37077 Göttingen, Germany;University of Fribourg, Institute for Zoology, Pérolles, CH-1700 Fribourg, Switzerland;University of Berne, Institute of Parasitology, PO Box 8466, CH-3001 Berne, Switzerland

关键词: Polyglutamylation;    Polyglycylation;    Posttranslational modification;    Tubulin;    Tyrosination;    Giardia lamblia;   

DOI  :  10.1016/S0014-5793(97)01436-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tubulin of Giardia lamblia, a representative of the oldest eukaryotes, was screened for posttranslational modifications. Mass spectrometry of the carboxy-terminal peptides documents a large number of variants. Both α- and β-tubulin show polyglycylation with up to 20 and 15 extra glycyl residues respectively. Minor variants show a low level of glutamylation without or with glycylation. The glutamylation-specific antibody GT335 detects α- and β-tubulin in immunoblots. The terminal tyrosine is fully retained in α-tubulin, which is completely acetylated at Lys-40. Thus except for the detyrosination/tyrosination cycle all posttranslational modifications known for higher eukaryotes are already present in Giardia.

【 授权许可】

Unknown