Initial description of the developing soybean seed protein Lys-Nε-acetylome

Global Lysine Acetylome Analysis of Desiccated Somatic Embryos of Picea asperata

“…By searching these acetylated peptides identified against the previous proteome dataset of the embryos during PDT, we validated 1079 unique acetylation sites in 556 acetylated proteins (Figure 2B and Supplementary Table S1). Previously, plant lysine acetylome studies identified 74 acetylated proteins in A. thaliana (Finkemeier et al, 2011), 31 in S. tuberosum (Xing and Poirier, 2012), 97 in V. vinifera (Melo-Braga et al, 2012), 121 in G. max (Smith-Hammond et al, 2014b), 358 in P. sativum (Smith-Hammond et al, 2014a), 684 in F. ananassa (Fang et al, 2015), 227 in T. aestivum (Zhang et al, 2016), and 716 in O. sativa (Xiong et al, 2016). These different numbers are mainly due to the different intrinsic acetylation levels of the proteins among the various species.…”

“…The preferred amino acid residues surrounding LysAc sites have been identified in plants (Finkemeier et al, 2011; Melo-Braga et al, 2012; Nallamilli et al, 2014; Smith-Hammond et al, 2014a,b; Fang et al, 2015; He et al, 2016; Xiong et al, 2016; Zhang et al, 2016). To explore the conserved LysAc motifs of the desiccated somatic embryos of P. asperata , we used the Motif-X program to search for conserved sequence motifs in all of the validated 1079 acetylated-lysine sites.…”

“…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.…”

In silico analysis of protein Lys-N𝜀-acetylation in plants

“…It has been reported that PKA sites are significantly enriched in ordered regions of mammalian proteins and depleted in regions of ISD (Choudhary et al, 2009), that PKA sites are equally distributed in ordered and disordered regions (Gao and Xu, 2011), and that PKA sites preferentially occur in regions of ISD in Toxoplasma gondii tachyzoite proteins (Xue et al, 2013). We observed that versus all Lys residues in our soybean database, PKA was approximately twice as likely to occur in long ISD-regions (Smith-Hammond et al, 2014b). If, as has recently been proposed (Cumberworth et al, 2013), regions of ISD are important in mediating protein interactions, then PTM of residues within regions of ISD might explain the basis for multiple layers of regulation (Nishi et al, 2013).…”

“…These include 131 A. thaliana proteins (155 sites; Finkemeier et al, 2011; Wu et al, 2011), 97 Vitis vinifera berry proteins (138 sites; Melo-Braga et al, 2012), 121 proteins (190 sites) from developing Glycine max cotyledons (Smith-Hammond et al, 2014b), and 31 proteins (35 sites) from Solanum tuberosum mitochondrial proteins (Salvato et al, 2014). Even after results from work in progress are added; 90 A. thaliana mitochondrial proteins (174 sites; König et al, 2014a), and 358 Pisum sativum proteins (664 sites; Smith-Hammond et al, 2014a), the extant number of PKA proteins is small in comparison to P-proteins and only five species have been examined.…”