Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  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.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Zeitschriftenartikel

Dateien

einblenden: Dateien
ausblenden: Dateien
:
949.full.pdf (Verlagsversion), 4MB
Name:
949.full.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
© 2017 The Authors. Published under the terms of the CC BY 4.0 license
:
949.figures-only#fig-data-supplementary-materials (Ergänzendes Material), 212KB
Name:
949.figures-only#fig-data-supplementary-materials
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
text/html / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:

Urheber

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

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: 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.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2017-10-23
 Publikationsstatus: Online veröffentlicht
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000416160000006
DOI: 10.15252/msb.20177819
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Molecular Systems Biology
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: London : Nature Pub. Group
Seiten: - Band / Heft: 13 (10) Artikelnummer: 949 Start- / Endseite: - Identifikator: ISSN: 1744-4292
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000021290