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

Colin L. Smith-Hammond, Kirby N. Swatek, Mark L. Johnston, Jay J. Thelen, Jan A. Miernyk
Journal of proteomics 2014 v.96 pp. 56-66
Arabidopsis thaliana, post-translational modification, lysine, Glycine max, protein folding, proteome, soybeans, cotyledons, cAMP-dependent protein kinase, acetylation, RNA, plant proteins
Characterization of the myriad protein posttranslational modifications (PTM) is a key aspect of proteome profiling. While there have been previous studies of the developing soybean seed phospho-proteome, herein we present the first analysis of protein Lys-Ne-acetylation (PKA) in this system. In recent years there have been reports that PKA is widespread, affecting thousands of proteins in diverse species from bacteria to mammals. Recently, a preliminary description of the protein lysine-acetylome from the reference plant Arabidopsis thaliana has been reported. Using a combination of immunoenrichment and mass spectrometry-based techniques, we have identified 190 sites of lysine acetylation in 120 distinct proteins from developing soybean (Glycine max (L.) Merr., cv. Jack) cotyledons, which more than doubles the number of known plant Ne-lysine-acetylation sites. Results of functional annotation indicate acetyl-proteins are involved with a host of cellular activities. In addition to the histones, and other proteins involved in RNA synthesis and processing, acetyl-proteins participate in signaling, protein folding, and a plethora of metabolic processes. Results from in silico localization indicate that lysine-acetylated proteins are present in all major subcellular compartments. In toto, our results establish that developing soybean cotyledons will be a useful system for functional analysis of PKA.