Abstract
Rocky desertification is a bottleneck that reduces ecological and environmental security in karst areas. Paper mulberry, a unique deciduous tree, shows good performance in rocky desertification areas. Its resistance mechanisms are therefore of high interest. In this study, a lysine acetylation proteomics analysis of paper mulberry seedling leaves was conducted in combination with the purification of acetylated protein by high-precision nano LC-MS/MS. We identified a total of 7130 acetylation sites in 3179 proteins. Analysis of the modified sites showed a predominance of nine motifs. Six positively charged residues: lysine (K), arginine (R), and histidine (H), serine (S), threonine (T), and tyrosine (Y) occurred most frequently at the +1 position, phenylalanine (F) was both detected both upstream and downstream of the acetylated lysines; and the sequence logos showed a strong preference for lysine and arginine around acetylated lysines. Functional annotation revealed that the identified enzymes were mainly involved in translation, transcription, ribosomal structure and biological processes, showing that lysine acetylation can regulate various aspects of primary carbon and nitrogen metabolism and secondary metabolism. Acetylated proteins were enriched in the chloroplast, cytoplasm, and nucleus, and many stress response-related proteins were also discovered to be acetylated, including PAL, HSP70, and ERF. HSP70, an important protein involved in plant abiotic and disease stress responses, was identified in paper mulberry, although it is rarely found in woody plants. This may be further examined in research in other plants and could explain the good adaptation of paper mulberry to the karst environment. However, these hypotheses require further verification. Our data can provide a new starting point for the further analysis of the acetylation function in paper mulberry and other plants.
Highlights
Ecosystem degradation and soil erosion are major problems that restrict the regional economy in karst areas
Posttranslational modifications (PTMs) of histone are well-known for their critical roles in cellular pathways, as they can change the physicochemical properties of proteins and affect their activity and stability [3, 4]
Paper mulberry is a perennial tree species characterized by a higher growth rate and greater adaptability to adverse environments than other species
Summary
Ecosystem degradation and soil erosion are major problems that restrict the regional economy in karst areas. A comprehensive examination of the lysine acetylation targets in paper mulberry based on proteomics analyses vegetation can be challenging because of these problems. Protein regulation encompasses multilayered and interconnected transcriptional and translational processes [1]. This process begins with transcription from DNA and the splicing of genes into RNA molecules, which are subsequently translated into polypeptides later [2]. Posttranslational modifications (PTMs) of histone are well-known for their critical roles in cellular pathways, as they can change the physicochemical properties of proteins and affect their activity and stability [3, 4]. Among PTMs, lysine acetylation was first discovered on histone tails where chromatin structure and gene expression are regulated. Changes in cellular lysine acetylation status can alter metabolic enzyme activity and provide an adaptive mechanism for specific metabolic changes in cells [6]
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