Post-translational modifications of α-tubulin in Zea mays L. are highly tissue specific View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-01

AUTHORS

Wei Wang, Rita Vignani, Monica Scali, Elisabetta Sensi, Mauro Cresti

ABSTRACT

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. More... »

PAGES

460-465

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00425-003-1122-4

DOI

http://dx.doi.org/10.1007/s00425-003-1122-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046789050

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/14534789


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