Abstract:
:Several types of post-translational modifications contribute to the high level of tubulin heterogeneity in the brain. An important modification is glutamylation of the major brain-specific isotypes, such as class Ia/b of alpha-tubulin and classes II and III of beta-tubulin. Here we describe experiments to determine if additional, minor tubulin isotypes, expressed in adult mouse brain, could also be glutamylated. Purified tubulin from adult mouse brain was cleaved with thermolysin. Proteolytically released carboxy-terminal peptides of both alpha- and beta-tubulin were isolated by sequential anion exchange and reverse-phase column-chromatography. Anionic peptides were then characterized by amino acid sequencing and mass spectrometry. We show that brain-specific class IVa and constitutive class I beta-tubulin isotypes can be glutamylated, at Glu434 and Glu441, respectively.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Mary J,Redeker V,Le Caer JP,Promé JC,Rossier Jdoi
10.1016/0014-5793(94)01018-8subject
Has Abstractpub_date
1994-10-10 00:00:00pages
89-94issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(94)01018-8journal_volume
353pub_type
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