• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

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.

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.

Pubmed ID: 22404109

Authors

  • Tran HT
  • Nimick M
  • Uhrig RG
  • Templeton G
  • Morrice N
  • Gourlay R
  • DeLong A
  • Moorhead GB

Journal

The Plant journal : for cell and molecular biology

Publication Data

July 27, 2012

Associated Grants

  • Agency: Medical Research Council, Id: G1100713

Mesh Terms

  • Acetylation
  • Arabidopsis
  • Arabidopsis Proteins
  • Cell Nucleus
  • Cytosol
  • Histone Acetyltransferases
  • Histone Deacetylases
  • Microcystins
  • Microtubules
  • Phosphorylation
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Phosphatase 2
  • Recombinant Fusion Proteins
  • Tubulin