J Biol Chem 1996 Apr 26;27117:9928-33. doi: 10.1074/jbc.271.17.9928.

Posttranslational modifications in the C-terminal tail of axonemal tubulin from sea urchin sperm.

???displayArticle.abstract???
After proteolytic digestion of sperm tubulin from sea urchin Paracentrotus lividus, C-terminal peptides were isolated by chromatographic separations. The peptides were analyzed by Edman degradation and matrix-assisted laser desorption/ionization-time of flight mass spectrometry. About 70% of the isolated C-terminal peptides were unmodified. The remaining modified peptides have undergone a combination of numerous posttranslational modifications generating significant heterogeneity of sperm tubulin. alpha-Tubulin is modified by detyrosylation, release of the penultimate glutamate, polyglutamylation, and polyglycylation. Glycylation and glutamylation can coexist within one alpha-tubulin isoform. beta-Tubulin undergoes polyglycylation but was not observed to be polyglutamylated. The number of units posttranslationally added reaches 11 and 12 glycyl units on beta- and alpha-tubulin, respectively. This is different from the polyglycylation of axonemal tubulin in Paramecium cilia where up to 40 added glycyl units were observed both on alpha- and beta-tubulin.

???displayArticle.pubmedLink??? 8626629
???displayArticle.link??? J Biol Chem


Genes referenced: dnah3 LOC100887844 LOC594566 tubgcp2