Abstract
Protein lysine acetylation (Kac) is an important post-translational modification in both animal and plant cells. Global Kac identification has been performed at the proteomic level in various species. However, the study of Kac in oil and resource plant species is relatively limited. Soybean is a globally important oil crop and resouce plant. In the present study, lysine acetylome analysis was performed in soybean leaves with proteomics techniques. Various bioinformatics analyses were performed to illustrate the structure and function of these Kac sites and proteins. Totally, 3148 acetylation sites in 1538 proteins were detected. Motif analysis of these Kac modified peptides extracted 17 conserved motifs. These Kac modified protein showed a wide subcellular location and functional distribution. Chloroplast is the primary subcellular location and cellular component where Kac proteins were localized. Function and pathways analyses indicated a plenty of biological processes and metabolism pathways potentially be influenced by Kac modification. Ribosome activity and protein biosynthesis, carbohydrate and energy metabolism, photosynthesis and fatty acid metabolism may be regulated by Kac modification in soybean leaves. Our study suggests Kac plays an important role in soybean physiology and biology, which is an available resource and reference of Kac function and structure characterization in oil crop and resource plant, as well as in plant kingdom.
Highlights
Protein lysine acetylation (Kac) is an important post-translational modification in both animal and plant cells
Our study showed the central carbohydrate metabolism pathways, including EMP, TCA and phosphate pathway (PPP) may be influenced by Kac modification in soybean leaves (Fig. 4B)
The results indicated Kac was a rich Post-translational modifications (PTMs) in soybean leaf proteins
Summary
Protein lysine acetylation (Kac) is an important post-translational modification in both animal and plant cells. 2057 novel Kac sites corresponding to 959 proteins were discovered in a recent study[23] Another quantitative acetylome analysis in Arabidopsis organs and seedlings reported 909 acetylated proteins, of which 536 acetylated proteins showed changed abundance upon different experiment treatment c onditions[24]. Suspension cell, seed, leaves, anthers and whole seedling (root, shoot and leaf) were used as material to uncover the regulation role of Kac in plant physiology and biology; and a wide range of Kac sites and proteins numbers were reported in these studies due to diverse factors[25,26,27,28,29,30,31]. Revisable protein acetylation participated in immune response to virulent C. carbonum[35]
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