To further understand post-translational modifications (PTMs) of plant Î±-tubulin, post-translationally modified Î±-tubulin isoforms from selected tissues of Zea mays L. were examined using two-dimensional electrophoresis and immunoblotting. Except for polyglycylated tubulin, tyrosinated, detyrosinated, acetylated and polyglutamylated Î±-tubulin isoforms were all present in maize tissues. Tyrosinated Î±-tubulin was the predominant variant in all cases, with isoforms Î±1-Î±4 (Î±5) being the most common components. Leaves exhibited a striking difference in PTM patterns of Î±-tubulin isoforms compared to other tissues examined. In leaves, several major specific isoforms were highly modified by detyrosination, acetylation and polyglutamylation. In pollen and anthers, only the most abundant isoform Î±3 was acetylated to an appreciable extent, and no acetylated isoform was found in roots. Similarly, in pollen, anthers and roots, only Î±3 was appreciably polyglutamylated. Additionally, a detyrosinated isoform Î±6 was present in anthers and in leaves, while the tyrosinated isoform Î±6 seemed to be pollen specific. These results indicate that certain types of PTM of plant Î±-tubulin preferentially occur in a tissue-specific way.
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|Titolo:||Post-translational modifications of Î±-tubulin in Zea mays L. are highly tissue specific|
|Appare nelle tipologie:||1.1 Articolo in rivista|