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  Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis

Hartl, M., Fuessl, M., Boersema, P. J., Jost, J.-O., Kramer, K., Bakirbas, A., et al. (2017). Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis. Molecular Systems Biology, 13(10): 949. doi:10.15252/msb.20177819.

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 Creators:
Hartl, M.1, Author              
Fuessl, M.1, Author              
Boersema, Paul J.2, Author              
Jost, J.-O.1, Author
Kramer, K.1, Author              
Bakirbas, A.1, Author
Sindlinger, J.1, Author
Ploechinger, M.1, Author
Leister, D.1, Author
Uhrig, G.1, Author
Moorhead, G. B. G.1, Author
Cox, Jürgen2, Author              
Salvucci, M. E.1, Author
Schwarzer, D.1, Author
Mann, M.1, Author
Mann, Matthias2, Author              
Finkemeier, I.1, Author              
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2017-10-23
 Publication Status: Published online
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 Identifiers: ISI: 000416160000006
DOI: 10.15252/msb.20177819
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Title: Molecular Systems Biology
Source Genre: Journal
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Publ. Info: London : Nature Pub. Group
Pages: - Volume / Issue: 13 (10) Sequence Number: 949 Start / End Page: - Identifier: ISSN: 1744-4292
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000021290