Comprehensive Proteome Analyses of Lysine Acetylation in Tea leaves by sensing Nitrogen nutrition

Acetylation of lysine is a highly dynamic and reversibly regulated post-translational modification (PTM), which changes protein function in multiple ways [1]. As one of the most common PTMs to proteins in both eukaryotes and prokaryotes [1, 2], lysine acetylation occurred on either the α-amino group at the N-terminus of the protein or the ε-amino group on the side chain of lysine residues[3]. Since the first reveal of lysine acetylome in mammalian cells [4], acetylome in eukaryotes has been reported and the mechanistic studies indicated that lysine acetylation impacted various cellular processes including transcriptional regulation and metabolic stability [5-8]. In addition, a growing number of studies indicated that lysine acetylation widely existed in prokaryotes, and functional annotation showed lysine acetylation plays a crucial role in metabolic pathways, stress responses and enzymatic activity regulations in bacteria [9-11].