Posttranslational modifications of trichomonad tubulins; identification of multiple glutamylation sites

FEBS Letters

Schneider, André¹  Weber, Klaus²  Felleisen, Richard³  Plessmann, Uwe² 

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

关键词: Trichomonad;    Polyglutamylation;    Polyglycylation;    Posttranslational modification;    Tubulin;   

DOI  :  10.1016/S0014-5793(98)00644-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The α- and β-tubulins present in cytoskeletons of Tritrichomonas mobilensis are extensively glutamylated. Automated sequencing and mass spectrometry of the carboxyterminal peptides identifies 4 glutamylation sites in α- and 2 sites in β-tubulin. They are marked by asterisks in the terminal sequences GDE*E*E*E*DDG (α) and EGE*E*DEEAEA (β). This is the first report that tubulin glutamylation can occur at multiple sites. Although T. mobilensis has four flagellae the tubulins lack polyglycylation. Thus glycylation is not necessary for formation or function of axonemal microtubules. α-Tubulin is completely acetylated at lysine 40 and shows no tyrosine cycle. Peptide sequences establish two distinct β-tubulins.

【 授权许可】

Unknown