Tran, H.T., Nimick, M., Uhrig, R.G., Templeton, G., Morrice, N., Gourlay, R., DeLong, A. and Moorhead, G.B.G. (2012) Arabidopsis thaliana histone deacetylase 14 (HDA14) is an α-tubulin deacetylase that associates with PP2A and enriches in the microtubule fraction with the putative histone acetyltransferase ELP3. Plant Journal, 71(2), pp. 263-272. (doi: 10.1111/j.1365-313X.2012.04984.x)
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Abstract
It is now emerging that many proteins are regulated by a variety of covalent modifications. Using microcystin-affinity chromatography we have purified multiple protein phosphatases and their associated proteins from Arabidopsis thaliana. One major protein purified was the histone deacetylase HDA14. We demonstrate that HDA14 can deacetylate α-tubulin, associates with α/β-tubulin and is retained on GTP/taxol-stabilized microtubules, at least in part, by direct association with the PP2A-A2 subunit. Like HDA14, the putative histone acetyltransferase ELP3 was purified on microcystin-Sepharose and is also enriched at microtubules, potentially functioning in opposition to HDA14 as the α-tubulin acetylating enzyme. Consistent with the likelihood of it having many substrates throughout the cell, we demonstrate that HDA14, ELP3 and the PP2A A-subunits A1, A2 and A3 all reside in both the nucleus and cytosol of the cell. The association of a histone deacetylase with PP2A suggests a direct link between protein phosphorylation and acetylation.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Morrice, Dr Nicholas |
| Authors: | Tran, H.T., Nimick, M., Uhrig, R.G., Templeton, G., Morrice, N., Gourlay, R., DeLong, A., and Moorhead, G.B.G. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Cancer Sciences |
| Journal Name: | Plant Journal |
| ISSN: | 0960-7412 |
| ISSN (Online): | 1365-313X |
| Published Online: | 02 May 2012 |
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