Phosphorylation is the most extensive post-translational modification of proteins and thus regulates plant growth. However, the regulatory mechanism of phosphorylation modification on the growth of tea plants caused by organic nitrogen is still unclear. In order to explore the phosphorylation modification mechanism of tea plants in response to organic nitrogen, we used glycine as the only nitrogen source and determined and analyzed the phosphorylated proteins in tea plants by phosphoproteomic analysis. The results showed that the phosphorylation modification induced by glycine-supply played important roles in the regulation of energy metabolism in tea roots and amino acid metabolism in tea leaves. In roots, glycine-supply induced dephosphorylation of proteins, such as fructose-bisphosphate aldolase cytoplasmic isozyme, glyceraldehyde-3-phosphate dehydrogenase, and phosphoenolpyruvate carboxylase, resulted in increased intensity of glycolysis and decreased intensity of tricarboxylic acid cycle. In leaves, the glycine-supply changed the phosphorylation levels of glycine dehydrogenase, aminomethyltransferase, glutamine synthetase, and ferredoxin-dependent glutamate synthase, which accelerated the decomposition of glycine and enhanced the ability of ammonia assimilation. In addition, glycine-supply could improve the tea quality by increasing the intensity of amino acids, such as theanine and alanine. This research clarified the important regulatory mechanism of amino acid nitrogen on tea plant growth and development through protein phosphorylation.
Keywords: glycine; metabolic pathway; organic nitrogen; protein phosphorylation; tea plants.