Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis

• DOI: 10.15252/msb.20177819
• Publication Date: 2017-10-24T00:11:20Z
• Authors: Markus Hartl; Magdalena Füßl; Paul J Boersema; Jan‐Oliver Jost; Katharina Kramer; Ahmet Bakirbas; Julia Sindlinger; Magdalena Plöchinger; Dario Leister; Glen Uhrig; Greg BG Moorhead; Jürgen Cox; Michael E Salvucci; Dirk Schwarzer; Matthias Mann; Iris Finkemeier
• Keywords: Histone deacetylase 5; SAP30; Histone deacetylase 2; HDAC11; HDAC4

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