These authors contributed equally to this manuscript.
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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
Article first published online: 2 MAY 2012
DOI: 10.1111/j.1365-313X.2012.04984.x
© 2012 The Authors. The Plant Journal © 2012 Blackwell Publishing Ltd
Additional Information
How to Cite
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. The Plant Journal, 71: 263–272. doi: 10.1111/j.1365-313X.2012.04984.x
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These authors contributed equally to this manuscript.
Publication History
- Issue published online: 26 JUL 2012
- Article first published online: 2 MAY 2012
- Accepted manuscript online: 8 MAR 2012 03:54AM EST
- Received 23 December 2008; revised 9 February 2012; accepted 4 March 2012; published online 2 May 2012.
Keywords:
- histone deacetylase;
- histone acetyltransferase;
- PP2A;
- tubulin;
- ELP3;
- HDA14
Summary
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.