Polyglycylation of tubulin in the diplomonad Giardia lamblia, one of the oldest eukaryotes.
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 alpha-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.
Weber
K
K
Max-Planck-Institute for Biophysical Chemistry, Department of Biochemistry, Goettingen, Germany.
Schneider
A
A
Müller
N
N
Plessmann
U
U
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D016829:Giardia lamblia / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D015800:Protozoan Proteins / Q000378:metabolism; D014404:Tubulin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D003598:Cytoskeletal Proteins; D015800:Protozoan Proteins; D014404:Tubulin; C038207:giardin protein, Giardia lamblia