Lysine acetylation contributes to artificial ageing in wheat (Triticum aestivum L.) seeds.

In this work, the role of protein acetylation modification in wheat aging was studied using TMT labelling, enrichment of acetylation peptides and quantitative proteomics strategy of high-resolution liquid chromatography-mass spectrometry. A total of 1663 acetylation sites were identified on 892 proteins, of which 1526 sites on 830 proteins had quantitative information. Furthermore, 255 differentially acetylated sites were identified, of which 135 sites were up-regulated and 120 sites were down-regulated.