Abstract
Partial desiccation treatment (PDT) promotes the germination capacity of conifer somatic embryos. Lysine acetylation (LysAc) is a dynamic and reversible post-translational modification that plays a key role in many biological processes including metabolic pathways and stress response. To investigate the functional impact of LysAc in the response of Picea asperata somatic embryos to PDT, we performed a global lysine acetylome analysis. Here, combining antibody-based affinity enrichment and high-resolution mass spectrometry, we identified and validated 1079 acetylation sites in 556 acetylated proteins from P. asperata somatic embryos during PDT. These data represent a novel large-scale dataset of lysine-acetylated proteins from the conifer family. Intensive bioinformatics analysis of the Gene Ontology of molecular functions demonstrated that lysine-acetylated proteins were mainly associated with binding, catalytic activities, and structural molecular activities. Functional characterization of the acetylated proteins revealed that in the desiccated somatic embryos, LysAc is mainly involved in the response to stress and central metabolism. Accordingly, the majority of these interacting proteins were also highly enriched in ribosome, proteasome, spliceosome, and carbon metabolism clusters. This work provides the most comprehensive profile of LysAc for a coniferous species obtained to date and facilitates the systematic study of the physiological role of LysAc in desiccated somatic embryos of P. asperata.
Highlights
Lysine acetylation (LysAc) is a ubiquitous, reversible and highly conserved post-translational modification (PTM) of both histones and non-histone proteins of prokaryotes and eukaryotes (Kim et al, 2006; Choudhary et al, 2009; Weinert et al, 2013)
Somatic embryogenesis has been achieved in a variety of coniferous species (Klimaszewska et al, 2016)
In this study, using antibody-based affinity enrichment and high-resolution mass spectrometry (MS), we comprehensively investigated the lysine acetylome in P. asperata desiccated somatic embryos
Summary
Lysine acetylation (LysAc) is a ubiquitous, reversible and highly conserved post-translational modification (PTM) of both histones and non-histone proteins of prokaryotes and eukaryotes (Kim et al, 2006; Choudhary et al, 2009; Weinert et al, 2013). This modification represents an effective approach for transcriptional regulation and modulates diverse properties of proteins, such as protein activity and localization and protein-nucleic acid and protein-protein interactions (Arif et al, 2010). Functional annotation demonstrated that LysAc is mainly associated with regulation of enzymatic activities, metabolic pathways, and stress responses (Tootle and Rebay, 2005; Zhang et al, 2009; Liu et al, 2016)
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