Polyglycylation of tubulin in the diplomonad Giardia lamblia, one of the oldest eukaryotes

FEBS Letters

Schneider, André²  Weber, Klaus³  Müller, Norbert¹  Plessmann, Uwe³ 

[1] University of Berne, Institute of Parasitology, PO Box 8466, CH 3001 Berne, Switzerland;University of Fribourg, Institute for Zoology, Pérolles, CH 1700 Fribourg, Switzerland;Max-Planck-Institute for Biophysical Chemistry, Department of Biochemistry, PO Box 2841, D-37018 Goettingen, Germany

关键词: Flagella;    Polyglutamylation;    Polyglycylation;    Post-translational modification;    Tubulin;    Tyrosination;    HPLC;    high-performance liquid chromatography;    MALDI;    matrix-assisted laser desorption ionization;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(96)00848-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have searched for post-translational modifications in tubulin of the diplomonad Giardia lamblia, which is a representative of the earliest branches in eukaryotic evolution. The carboxyterminal peptide of α-tubulin was isolated and characterized by automated sequencing and mass spectrometry. Some 60% of the peptide is unmodified, while the remainder shows various degrees of polyglycylation. The number of glycyl residues in the lateral side chain ranges from 2 to 23. All peptide species encountered end with alanine-tyrosine, indicating the absence of a detyrosination/tyrosination cycle. We conclude that tubulin-specific polyglycylation could be as old as tubulin and axonemal structures.

【 授权许可】

Unknown