Publication Information
Hartl et al., 2017
Abstract
Mol Syst Biol. 2017 Oct 23;13(10):949. doi: 10.15252/msb.20177819.
Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins
in Arabidopsis.
Hartl M(1)(2)(3), Füßl M(1)(2)(4), Boersema PJ(5), Jost JO(6), Kramer K(1),
Bakirbas A(1)(4), Sindlinger J(6), Plöchinger M(2), Leister D(2), Uhrig G(7),
Moorhead GB(7), Cox J(5), Salvucci ME(8), Schwarzer D(6), Mann M(5), Finkemeier
I(9)(2)(4).
Author information:
(1)Plant Proteomics, Max Planck Institute for Plant Breeding Research, Cologne,
Germany.
(2)Plant Molecular Biology, Department Biology I, Ludwig-Maximilians-University
Munich, Martinsried, Germany.
(3)Mass Spectrometry Facility, Max F. Perutz Laboratories (MFPL), Vienna
Biocenter (VBC), University of Vienna, Vienna, Austria.
(4)Plant Physiology, Institute of Plant Biology and Biotechnology, University of
Muenster, Muenster, Germany.
(5)Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry,
Martinsried, Germany.
(6)Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen,
Germany.
(7)Department of Biological Sciences, University of Calgary, Calgary, AB,
Canada.
(8)US Department of Agriculture, Agricultural Research Service, Arid-Land
Agricultural Research Center, Maricopa, AZ, USA.
(9)Plant Proteomics, Max Planck Institute for Plant Breeding Research, Cologne,
Germany iris.finkemeier@uni-muenster.de.
Histone deacetylases have central functions in regulating stress defenses and
development in plants. However, the knowledge about the deacetylase functions is
largely limited to histones, although these enzymes were found in diverse
subcellular compartments. 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.
© 2017 The Authors. Published under the terms of the CC BY 4.0 license.
DOI: 10.15252/msb.20177819
PMCID: PMC5658702
PMID: 29061669 [Indexed for MEDLINE]
