Acetylome profiling reveals extensive involvement of lysine acetylation in the conversion of muscle to meat
Acetylome profiling reveals extensive involvement of lysine acetylation in the conversion of muscle to meat
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乙酰组分析揭示赖氨酸乙酰化广泛参与肌肉向肉类的转化
DOI：
10.1016/j.jprot.2019.103412
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发表时间：
2019-08-15
影响因子：
3.3
通讯作者：
Shen, Qingwu W.
中科院分区：
文献类型：
--
作者：
Jiang, Shengwang;Liu, Yisong;Shen, Qingwu W.
蛋白质赖氨酸乙酰化是一种翻译后修饰，可调控基因表达、代谢、细胞信号传导和疾病，但其在宰后肉质发育中的意义尚不清楚。在本研究中，定量蛋白质组学分析进行了轮廓在24小时PM猪肌肉乙酰组。在猪肌肉中共鉴定出163个蛋白质的595个乙酰化位点，其中460个位点分布于110个蛋白质，在肌肉向肉的转化过程中乙酰化水平发生了显著变化。肌肉蛋白质的动态乙酰化/脱乙酰化与PM肌肉中关键的化学-生物物理变化密切相关。生物信息学分析表明，蛋白质赖氨酸乙酰化可能通过调节糖酵解和肌肉pH值、细胞应激反应和凋亡、肌肉收缩和尸僵、钙信号和蛋白质水解、IMP合成和风味形成，甚至色素蛋白和肉色的稳定性来调控宰后肉质的发展。本研究首次对PM肌肉中蛋白质赖氨酸乙酰化进行了综述，并揭示了其在肌肉向肉转化中的意义。未来探索蛋白质赖氨酸乙酰化在特定位点的确切作用将进一步加深我们对潜在机制的理解，并有助于肉品质量控制。结果表明，肌肉蛋白质的动态乙酰化/脱乙酰化与肌肉的宰后变化密切相关，并影响生肉的最终品质。与葡萄糖代谢和肌肉收缩相关的蛋白质是宰后猪肌肉中鉴定的两个最大的乙酰蛋白簇。同时，在猪死后肌肉中鉴定了参与细胞凋亡、钙信号传导和IMP合成的乙酰蛋白网络。我们的研究结果表明，蛋白质赖氨酸乙酰化调节肌肉到肉的转换。它可能通过调节宰后糖酵解、细胞凋亡、钙信号、尸僵、肉风味物质的合成和肉的嫩化来调控肉质的发育。我们的研究拓宽了我们对调节死后肌肉转化为肉类和最终肉质发育的生物化学的理解，这可能有助于未来的肉质控制。
Protein lysine acetylation is an post-translational modification that regulates gene expression, metabolism, cell signaling, and diseases, but its implication in the postmortem (PM) meat quality development is basically unclear. In the present study, a quantitative proteomic analysis was conducted to profile acetylome in porcine muscle within 24 h PM. In total 595 acetylation sites assigned to 163 proteins were identified in porcine muscle, of which 460 sites distributing to 110 proteins significantly changed in acetylation levels in the conversion of muscle to meat. The dynamic acetylation/deacetylaion of muscle proteins was closely associated with critical chemical-biophysical changes in PM muscle. Bioinformatic analysis revealed that protein lysine acetylation likely regulated postmortem meat quality development by regulating glycolysis and muscle pH, cell stress reponse and apoptosis, muscle contraction and rigor mortis, calcium signaling and proteolysis, IMP synthesis and meat flavor development, and even the stability of pigment proteins and meat color. This study provided the first overview of protein lysine acetylation in PM muscle and revealed its significance in the conversion of muscle to meat. Future exploration of the exact role of protein lysine acetylation at specific sites will further our understanding regarding the underlying mechanisms and be helpful for meat quality control.Significance: This is the first analysis of acetylome in farm animal and postmortem muscle. Our data showed that the dynamic acetylation/deacetylation of muscle proteins was closely related to the postmortem changes of muscle that affect the final quality of raw meat. Proteins related to glucose metabolism and muscle contraction were the two largest clusters of acetylproteins identified in postmortem porcine muscle. Networks of acetylproteins involved in apoptosis, calcium signaling and IMP synthesis were identified in postmortem porcine muscle at the same time. Our results revealed that protein lysine acetylation regulated the conversion of muscle to meat. It likely regulated meat quality development by regulating postmortem glycolysis, mitochondrion initiated cell apoptosis, calcium signaling, rigor mortis, meat flavor compound sysnthesis and meat tenderization. Our study broadened our understanding of the biochemistry regulating the postmortem conversion of muscle to meat and final meat quality development, which may be helpful for future meat quality control.