Mammalian Sperm Tubulin: An Exceptionally Large Number of Variants Based on Several Posttranslational Modifications |
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Authors: | Uwe Plessmann and Klaus Weber |
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Affiliation: | (1) Department of Biochemistry, Max Planck Institute for Biophysical Chemistry, P.O. Box 2841, D-37018 Goettingen, Germany |
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Abstract: | Extraction of demembranated bull sperm flagella by SDS was used to maximize tubulin solubilization. The - and -tubulin separated by SDS-PAGE were treated with endoproteinases LysC and AspN, respectively. Carboxy-terminal fragments were isolated by Mono Q chromatography and reversed-phase HPLC. Automated sequencing and mass spectrometry revealed an astonishingly high number of tubulin variants. Many variants were due to polyglutamylation and in particular to polyglycylation. The number of side-chain glycyl residues ranged from 0 to 28 in and 0 to 15 in . Corresponding values for side-chain glutamyl residues were 0–6 in and 0–3 in . Additional variability was based on carboxy-terminal detyrosination and partial loss of the penultimate glutamate. A major glycylation site in - and -tubulin was mapped. Some variants seem to display both glycyl and glutamyl side chains. |
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Keywords: | Bull sperm polyglycylation polyglutamylation posttranslational modification tubulin |
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