Posttranslational modifications of trichomonad tubulins; identification of multiple glutamylation sites.
The alpha- and beta-tubulins present in cytoskeletons of Tritrichomonas mobilensis are extensively glutamylated. Automated sequencing and mass spectrometry of the carboxyterminal peptides identifies 4 glutamylation sites in alpha- and 2 sites in beta-tubulin. They are marked by asterisks in the terminal sequences GDE*E*E*E*DDG (alpha) and EGE*E*DEEAEA (beta). 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. Alpha-tubulin is completely acetylated at lysine 40 and shows no tyrosine cycle. Peptide sequences establish two distinct beta-tubulins.
Schneider
A
A
University of Fribourg, Institute of Zoology, Pérolles, Switzerland.
Plessmann
U
U
Felleisen
R
R
Weber
K
K
D000595:Amino Acid Sequence; D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism; D018698:Glutamic Acid / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D017421:Sequence Analysis; D014244:Trichomonas / Q000378:metabolism*; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism*
D010446:Peptide Fragments; D014404:Tubulin; D018698:Glutamic Acid