Polyglycylation of Tubulin: A Posttranslational Modification in Axonemal Microtubules

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 α and β...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1994-12, Vol.266 (5191), p.1688-1691
Main Authors: Redeker, Virginie, Levilliers, Nicolette, Schmitter, Jean-Marie, Le Caer, Jean-Pierre, Rossier, Jean, Adoutte, André, Bré, Marie-Hélène
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cilia
Cilia - chemistry
Cilia - metabolism
Cilia - ultrastructure
Contractile proteins
Elution
Fundamental and applied biological sciences. Psychology
Glutamic Acid - metabolism
Glycine - analysis
Glycine - metabolism
Holoproteins
Isotypes
Mass Spectrometry
Mass spectroscopy
Microtubules
Microtubules - chemistry
Microtubules - metabolism
Microtubules - ultrastructure
Molecular ions
Molecular Sequence Data
Paramecium
Paramecium - metabolism
Paramecium - ultrastructure
Peptides - analysis
Peptides - metabolism
Post translational modification
Protein Processing, Post-Translational
Proteins
Solvents
Tubulin
Tubulin - analysis
Tubulin - chemistry
Tubulin - metabolism
Tubulins
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Summary: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 α and β tubulin subunits, were modified by polyglycylation, containing up to 34 glycyl units covalently bound to the γ 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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.7992051