Post-translational modifications of ?-tubulin in Zea mays L. are highly tissue specific
Autor: | Mauro Cresti, Rita Vignani, Monica Scali, E. Sensi, Wei Wang |
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Rok vydání: | 2004 |
Předmět: |
Gene isoform
Immunoblotting Stamen Flowers macromolecular substances Plant Science Biology Plant Roots Zea mays Isozyme Tubulin Microtubule Detyrosination Genetics Protein Isoforms Polyglutamylation Plant Proteins Zea Plant Leaves α-tubulin isoforms Post-translational modification Biochemistry Organ Specificity Acetylation biology.protein Pollen Electrophoresis Polyacrylamide Gel Protein Processing Post-Translational |
Zdroj: | Planta. 218:460-465 |
ISSN: | 1432-2048 0032-0935 |
DOI: | 10.1007/s00425-003-1122-4 |
Popis: | To further understand post-translational modifications (PTMs) of plant alpha-tubulin, post-translationally modified alpha-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 alpha-tubulin isoforms were all present in maize tissues. Tyrosinated alpha-tubulin was the predominant variant in all cases, with isoforms alpha1-alpha4 (alpha5) being the most common components. Leaves exhibited a striking difference in PTM patterns of alpha-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 alpha3 was acetylated to an appreciable extent, and no acetylated isoform was found in roots. Similarly, in pollen, anthers and roots, only alpha3 was appreciably polyglutamylated. Additionally, a detyrosinated isoform alpha6 was present in anthers and in leaves, while the tyrosinated isoform alpha6 seemed to be pollen specific. These results indicate that certain types of PTM of plant alpha-tubulin preferentially occur in a tissue-specific way. |
Databáze: | OpenAIRE |
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