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dc.contributor.author
Hartl, Markus
dc.contributor.author
Füßl, Magdalena
dc.contributor.author
Boersema, Paul J.
dc.contributor.author
Jost, Jan-Oliver
dc.contributor.author
Kramer, Katharina
dc.contributor.author
Bakirbas, Ahmet
dc.contributor.author
Sindlinger, Julia
dc.contributor.author
Plöchinger, Magdalena
dc.contributor.author
Leister, Dario
dc.contributor.author
Uhrig, Glen
dc.contributor.author
Moorhead, Greg B.G.
dc.contributor.author
Cox, Jürgen
dc.contributor.author
Salvucci, Michael E.
dc.contributor.author
Schwarzer, Dirk
dc.contributor.author
Mann, Matthias
dc.contributor.author
Finkemeier, Iris
dc.date.accessioned
2017-12-13T13:28:07Z
dc.date.available
2017-11-08T04:35:51Z
dc.date.available
2017-12-13T13:28:07Z
dc.date.issued
2017-10-01
dc.identifier.other
10.15252/msb.20177819
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/205791
dc.identifier.doi
10.3929/ethz-b-000205791
dc.description.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.
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Arabidopsis
en_US
dc.subject
Histone deacetylases
en_US
dc.subject
lysine acetylation
en_US
dc.subject
photosynthesis
en_US
dc.subject
RuBisCO activase
en_US
dc.title
Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2017-10-23
ethz.journal.title
Molecular Systems Biology
ethz.journal.volume
13
en_US
ethz.journal.issue
10
en_US
ethz.pages.start
949
en_US
ethz.size
16 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.date.deposited
2017-11-08T04:35:56Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-12-13T13:28:11Z
ethz.rosetta.lastUpdated
2018-11-06T05:31:44Z
ethz.rosetta.versionExported
true
ethz.COinS
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