Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules
| Autor: | J.P. Le Caer, Jérôme Rossier, André Adoutte, Jean-Marie Schmitter, Nicolette Levilliers, Marie-Hélène Bré, Virginie Redeker |
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| Rok vydání: | 1994 |
| Předmět: |
Axoneme
Multidisciplinary Paramecium Edman degradation Molecular Sequence Data Glycine Glutamic Acid macromolecular substances Biology Microtubules Mass Spectrometry Tubulin Polyglycylation Biochemistry Microtubule Detyrosination biology.protein Animals Amino Acid Sequence Cilia Peptides Peptide sequence Polyglutamylation Protein Processing Post-Translational |
| Zdroj: | Science (New York, N.Y.). 266(5191) |
| ISSN: | 0036-8075 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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