Characterization of HD2C and its interaction with novel partners in Arabidopsis thaliana

[Truncated abstract] Histone deacetylases are known to bind a variety of targets and interacting proteins which are responsible for determining its activity in a temporal and spatial context. Here, Bimolecular Fluorescent Complementation (BiFC) assays were used to analyse putative interactions of the plant specific histone deacetylase HD2C isoform from Arabidopsis thaliana. Specifically, HD2C was shown to form homo- and hetero-dimers through interaction with other HD2 isoforms; it was shown to interact with both epsilon and non-epsilon 14-3-3 isoforms; and lastly it was shown to interact with the transcription factor TGA6.

Localization of HD2C-GFP traced accumulation of HD2C to the nucleus and nucleolus of Arabidopsis leaf cells. This was evidently dynamic, as salt stress induced the HD2C-GFP to localize to the nucleolus. This was linked to HD2C dimers, which showed a similarly nucleolar localization pattern. The nuclear localization was shown to be dependent on an evolutionarily conserved KKAK motif.