Abstract
Axonemal tubulin exhibits a high degree of heterogeneity mostly due to several posttranslational modifications (PTM). The aim of this work was to chemically characterize the different PTM occurring in the C-terminal tail of axonemal tubulin purified from sea urchin, Paracentrotus lividus, spermatozoa. After its purification, tubulin was enzymatically cleaved. The C-terminal peptides were chromatographically isolated, first by anion exchange and then by reverse-phase HPLC. Peptides were characterized by their sequence, determined by Edman degradation, and by their mass, determined by MALDI-TOF/MS. The two major conclusions are that the majority of the isolated C-terminal peptides were unmodified and that polyglycylation and polyglutamylation can occur simultaneously on one molecule of α-tubulin.
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Mary, J., Redeker, V., Le Caer, JP. et al. Posttranslational Modifications of Axonemal Tubulin. J Protein Chem 16, 403–407 (1997). https://doi.org/10.1023/A:1026336722124
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DOI: https://doi.org/10.1023/A:1026336722124