ECB-ART-36691
J Protein Chem
1997 Jul 01;165:385-90. doi: 10.1023/a:1026332621215.
Show Gene links
Show Anatomy links
Mammalian sperm tubulin: an exceptionally large number of variants based on several posttranslational modifications.
???displayArticle.abstract???
Extraction of demembranated bull sperm flagella by SDS was used to maximize tubulin solubilization. The alpha- and beta-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 alpha and 0 to 15 in beta. Corresponding values for side-chain glutamyl residues were 0-6 in alpha and 0-3 in beta. Additional alpha variability was based on carboxy-terminal detyrosination and partial loss of the penultimate glutamate. A major glycylation site in alpha- and beta-tubulin was mapped. Some variants seem to display both glycyl and glutamyl side chains.
???displayArticle.pubmedLink??? 9246618
???displayArticle.link??? J Protein Chem
Genes referenced: LOC115925415 LOC594261 tubgcp2
References [+] :
Eddé,
Posttranslational glutamylation of alpha-tubulin.
1990, Pubmed