Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis

In this study, we determined the proteome-wide signatures of the RPD3/HDA1 class of histone deacetylases in Arabidopsis. Relative quantification of the changes in the lysine acetylation levels was determined on a proteome-wide scale after treatment of Arabidopsis leaves with deacetylase inhibitors apicidin and trichostatin A. We identified 91 new acetylated candidate proteins other than histones, which are potential substrates of the RPD3/HDA1-like histone deacetylases in Arabidopsis, of which at least 30 of these proteins function in nucleic acid binding. Furthermore, our analysis revealed that histone deacetylase 14 (HDA14) is the first organellar-localized RPD3/HDA1 class protein found to reside in the chloroplasts and that the majority of its protein targets have functions in photosynthesis. Finally, the analysis of HDA14 loss-of-function mutants revealed that the activation state of RuBisCO is controlled by lysine acetylation of RuBisCO activase under low-light conditions.

Source: Molecular Systems Biology - October 23, 2017 Category: Molecular Biology Authors: Hartl, M., Füssl, M., Boersema, P. J., Jost, J.-O., Kramer, K., Bakirbas, A., Sindlinger, J., Plöchinger, M., Leister, D., Uhrig, G., Moorhead, G. B., Cox, J., Salvucci, M. E., Schwarzer, D., Mann, M., Finkemeier, I. Tags: Methods & Resources, Plant Biology, Post-translational Modifications, Proteolysis & Proteomics Articles Source Type: research