Global analysis of lysine acetylation in strawberry leaves

Abstract

Protein lysine acetylation is a reversible and dynamic post-translational modification. It plays an important role in regulating diverse cellular processes including chromatin dynamic, metabolic pathways, and transcription in both prokaryotes and eukaryotes. Although studies of lysine acetylome in plants have been reported, the throughput was not high enough, hindering the deep understanding of lysine acetylation in plant physiology and pathology. In this study, taking advantages of anti-acetyllysine-based enrichment and high-sensitive-mass spectrometer, we applied an integrated proteomic approach to comprehensively investigate lysine acetylome in strawberry. In total, we identified 1392 acetylation sites in 684 proteins, representing the largest dataset of acetylome in plants to date. To reveal the functional impacts of lysine acetylation in strawberry, intensive bioinformatic analysis was performed. The results significantly expanded our current understanding of plant acetylome and demonstrated that lysine acetylation is involved in multiple cellular metabolism and cellular processes. More interestingly, nearly 50% of all acetylated proteins identified in this work were localized in chloroplast and the vital role of lysine acetylation in photosynthesis was also revealed. Taken together, this study not only established the most extensive lysine acetylome in plants to date, but also systematically suggests the significant and unique roles of lysine acetylation in plants.

Acetylome Profiling Reveals Extensive Lysine Acetylation of the Fatty Acid Metabolism Pathway in the Diatom Phaeodactylum tricornutum

“…S3) (Kac indicates the acetylated lysine, and * represents a random amino acid residue). Three of these motifs, enrichment of Y, H or F on the +1 position toward the C terminus appeared frequently as previously described (50,51). The motifs KacH, KacY, Kac*F and KacF were also reported in strawberry (50) Figure 2B).…”

“…Recent studies have found amino acid residue over-or under represented at particular positions surrounding the acetylated lysine site in plants (50,51) and bacteria (18,20,(52)(53)(54). In this study, we defined 17 significantly enriched acetylation site motifs from 1894 unique sites accounting for 81.5% of sites identified, namely LKacY, KacY, LKac, Kac*F, I*Kac*L, YKac, K****Kac, FKac, KacH, KacF, K***Kac, I*Kac, Kac*L, Kac*Y, KacW, K*****Kac, F**Kac (Figure 2A and supplemental Table S6), and they display distinct abundance (supplemental Fig.…”

Global Lysine Acetylome Analysis of Desiccated Somatic Embryos of Picea asperata

“…Proteins were extracted from somatic embryos using the method described previously (Fang et al, 2015; He et al, 2016). Briefly, the embryos were ground in liquid nitrogen.…”

“…PTM-104, PTM Biolabs, Inc.), performed at 4°C overnight with gentle shaking (Pan et al, 2014; Fang et al, 2015; He et al, 2016). The supernatant was then removed, and the beads were washed four times with NETN buffer and twice with ddH 2 O.…”

“…The first systematic studies of LysAc demonstrated that during Arabidopsis thaliana development, LysAc modification participates in the regulation of central metabolic enzymes (Finkemeier et al, 2011; Wu et al, 2011). Thereafter, analyses of the lysine acetylomes of Vitis vinifera (Melo-Braga et al, 2012), Oryza sativa (Nallamilli et al, 2014; He et al, 2016; Xiong et al, 2016), Pisum sativum (Smith-Hammond et al, 2014a), Glycine max (Smith-Hammond et al, 2014b), Fragaria ananassa (Fang et al, 2015), and Triticum aestivum (Zhang et al, 2016) revealed that lysine-acetylated proteins are involved in growth and development in many plant species. However, there are no available reports of research on LysAc in coniferous species.…”