Identification and quantification of HDA14-dependent substrates in the Arabidopsis thaliana leaf acetylome of plants grown under low-light conditions

ABSTRACT: Lysine acetylation is a common post-translational modification in eukaryotes and prokaryotes which is known to be involved in the regulation of various cellular processes, such as transcriptional activation, metabolic signaling, and energy homeostasis. Nevertheless, its role in plant primary metabolism, and photosynthesis in particular, is not well understood. Lysine acetylation is catalyzed by acetyltransferases (KATs) and removed by corresponding deacetylases (KDACs). The Arabidopsis thaliana genome encodes for at least 16 KATs and 18 KDACs, belonging to seven different gene families. The cellular functions of these enzymes have been explored only partially, describing effects of single enzymes and their interaction with specific targets. HDA14 is a KDAC expressed primarily in chloroplasts which suggests an involvement in the regulation of photosynthesis or related metabolic processes. In this dataset we aimed to identify substrates of the histone deacetylase 14 in a global manner by comparing the leaf lysine acetylome of a hda14 KO plant to a wild-type under low-light conditions. Proteins were extracted and digested using an adapted FASP procedure, peptides were dimethyl-labeled and lysine-acetylated peptides were antibody-enriched. Peptide identification and quantitative data analysis was carried out using MaxQuant.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Katharina Kramer  

LAB HEAD: Prof. Iris Finkemeier

PROVIDER: PXD006651 | Pride | 2017-10-25

REPOSITORIES: Pride