Class I and IVa β‐tubulin isotypes expressed in adult mouse brain are glutamylated

FEBS Letters

Redeker, Virginie²  Rossier, Jean²  Le Caer, Jean-Pierre²  Promé, Jean-Claude¹  Mary, Jean² 

[1] Laboratoire de Pharmacologie et Toxicologie Fondamentales, CNRS UPR 8221, 31077 Toulouse Cedex, France;Institut Alfred Fessard, CNRS UPR 2212, 91198 Gif-sur-Yvette Cedex, France

关键词: Glutamylation;    Tubulin isotype;    Mass spectrometry;    Post-translational modification;    DEAE;    diethylaminoethyl;    IEF;    isoelectro focusing;    HPLC;    high-performance liquid chromatography;    L-SIMS;    liquid second ion mass spectrometry;    MAPs;    microtubule associated proteins;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(94)01018-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α-tubulin and classes II and III of β-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 α- and β-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 β-tubulin isotypes can be glutamylated, at Glu⁴³⁴ and Glu⁴⁴¹, respectively.

【 授权许可】

Unknown