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Science 5 January 1990:
Vol. 247. no. 4938, pp. 83 - 85
DOI: 10.1126/science.1967194
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Articles

Science, Vol 247, Issue 4938, 83-85
Copyright © 1990 by American Association for the Advancement of Science

articles

Posttranslational glutamylation of alpha-tubulin

B Edde, J Rossier, JP Le Caer, E Desbruyeres, F Gros, and P Denoulet

Laboratoire de Biochimie Cellulaire, College de France, Paris.

The high degree of tubulin heterogeneity in neurons is controlled mainly at the posttranslational level. Several variants of alpha-tubulin can be posttranslationally labeled after incubation of cells with [3H]acetate or [3H]glutamate. Peptides carrying the radioactive moiety were purified by high-performance liquid chromatography. Amino acid analysis, Edman degradation sequencing, and mass spectrometric analysis of these peptides led to the characterization of a posttranslational modification consisting of the successive addition of glutamyl units on the gamma-carboxyl group of a glutamate residue (Glu445). This modification, localized within a region of alpha-tubulin that is important in the interactions of tubulin with microtubule-associated proteins and calcium, could play a role in regulating microtubule dynamics.


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