A posttranslational modification was detected in the carboxyl-terminal
region of axonemal tubulin from Paramecium. Tubulin carboxyl-terminal
peptides were isolated and analyzed by Edman degradation sequencing,
mass spectrometry, and amino acid analysis. All of the peptides, deriv
ed from both alpha and beta tubulin subunits, were modified by polygly
cylation, containing up to 34 glycyl units covalently bound to the gam
ma carboxyl group of glutamyl residues. This modification, present in
one of the most stable microtubular systems, may influence microtubule
stability or axoneme function, or both.