Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin deacetylase that associates with PP2A and enriches in the microtubule fraction with the putative histone acetyltransferase ELP3

作者：Tran Hue T; Nimick Mhairi; Uhrig R Glen; Templeton George; Morrice Nick; Gourlay Robert; DeLong Alison; Moorhead Greg B G^*

来源：Plant Journal, 2012, 71(2): 263-272.

DOI：10.1111/j.1365-313X.2012.04984.x

• histone deacetylase
• histone acetyltransferase
• PP2A
• tubulin
• ELP3
• HDA14

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 alpha-tubulin, associates with alpha/beta-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 alpha-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.

• 出版日期2012-7