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Science 9 December 1994:
Vol. 266. no. 5191, pp. 1688 - 1691
DOI: 10.1126/science.7992051
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Articles

Science, Vol 266, Issue 5191, 1688-1691
Copyright © 1994 by American Association for the Advancement of Science

articles

Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules

V Redeker, N Levilliers, JM Schmitter, JP Le Caer, J Rossier, A Adoutte, and MH Bre

Institut Alfred Fessard, CNRS Unite Propre de Recherche 2212, Gif-sur-Yvette, France.

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, derived from both alpha and beta tubulin subunits, were modified by polyglycylation, containing up to 34 glycyl units covalently bound to the gamma 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.


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