og:image: http://msb.embopress.org/sites/default/files/highwire/msb/13/10.cover-source.jpg citation_mjid: msb;13/10/949 article:published_time: 2017-10-01 og:site_name: Molecular Systems Biology citation_reference: citation_journal_title=Molecular Systems Biology;citation_journal_abbrev=Mol Syst Biol;citation_title=Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis;citation_pages=949-949;citation_volume=13;citation_year=2017;citation_issue=10;citation_pmid=29061669;citation_doi=10.15252/msb.20177819 citation_journal_title: Molecular Systems Biology type: article og:description: 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. ![][1] A comprehensive lysine acetylome profiling identifies new potential substrate proteins of the Arabidopsis RPD3/HDA1?KDACs with various subcellular localizations. HDA14 is identified as the first RPD3/HDA1?KDAC, which is active in organelles. Mol Syst Biol. (2017) 13: 949 [1]: /embed/graphic-1.gif citation_issn: 1744-4292 citation_full_html_url: http://msb.embopress.org/content/13/10/949.full citation_public_url: http://msb.embopress.org/content/13/10/949 dc:title: Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis | Molecular Systems Biology Content-Encoding: UTF-8 citation_pdf_url: http://msb.embopress.org/content/13/10/949.full.pdf citation_section: Articles citation_num_pages: 16 citation_fulltext_world_readable: DC.Identifier: 10.15252/msb.20177819 DC.Rights: © 2017 The Authors. Published under the terms of the CC BY 4.0 license. This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. citation_author: Markus Hartl citation_abstract_html_url: http://msb.embopress.org/content/13/10/949.abstract citation_issue: 10 HW.identifier: /msb/13/10/949.atom citation_doi: 10.15252/msb.20177819 citation_volume: 13 Content-Language: en Generator: Drupal 7 (http://drupal.org) citation_author_orcid: http://orcid.org/0000-0002-4970-7336 DC.AccessRights: open-access citation_publication_date: 2017/10/01 citation_title: Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis citation_author_institution: Max Planck Institute for Plant Breeding Research citation_publisher: EMBO Press citation_id: 13/10/949 title: Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis | Molecular Systems Biology DC.Description: 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. ![][1] A comprehensive lysine acetylome profiling identifies new potential substrate proteins of the Arabidopsis RPD3/HDA1?KDACs with various subcellular localizations. HDA14 is identified as the first RPD3/HDA1?KDAC, which is active in organelles. Mol Syst Biol. (2017) 13: 949 [1]: /embed/graphic-1.gif Content-Type-Hint: text/html; charset=utf-8 DC.Format: text/html DC.Publisher: EMBO Press DC.Contributor: Markus Hartl Content-Type: application/xhtml+xml; charset=UTF-8 X-Parsed-By: org.apache.tika.parser.DefaultParser og:type: article article:section: Articles citation_pmid: 29061669 citation_article_type: Research Article og:title: Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis citation_abstract:

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.

DC.Title: Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis issue_cover_image: http://msb.embopress.org/sites/default/files/highwire/msb/13/10.cover-source.jpg citation_firstpage: 949 citation_funding_source: citation_funder=Deutsche Forschungsgemeinschaft, Germany;citation_funder_id=http://dx.doi.org/10.13039/501100001659;citation_grant_number=FI?1655/1?1; HW.pisa: msb;13/10/949 DC.Language: en DC.Date: 2017-10-01 citation_access: all category: research-article og:url: http://msb.embopress.org/content/13/10/949 article_thumbnail: http://msb.embopress.org/content/msb/13/10/949/embed/icon-1.gif