Comprehensive study of protein phosphorylation, acetylation, ubiquitination and <i>S</i>-nitrosylation profiles in pre- and post-rigor meat

This study investigated the integrated atlas of protein phosphorylation, acetylation, ubiquitination and S-nitrosylation in pre-rigor (0.5 h) and post-rigor (5 d) lamb to interpret the roles of protein post-translational modifications (PTMs) during meat aging. The results showed that the most common PTMs in postmortem meat were phosphorylated proteins. PTMs regulation during the postmortem period altered proteins involved in metabolic pathways and muscle contraction. The phosphorylation and ubiquitination of proteins located in mitochondria and nuclear changed significantly between 0.5 h and 5 d postmortem. Gene set enrichment analysis (GSEA) revealed possible roles of total PTMs proteins, with a general downregulation of phosphorylation, acetylation and ubiquitination. There was a weak correlation in the lysine PTM of acetylation and ubiquitination at the same site in postmortem meat. Multiple PTMs of proteins in glycolysis, TCA cycle, muscle contraction and the calcium signaling pathway cooperatively regulate meat quality development from pre-rigor to post-rigor.