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Acetylation Modification Analysis and Omics Techniques for Understanding Cellular Function and Disease Mechanisms

Acetylation modification analysis, when combined with protein or metabolite analysis, provides a powerful tool for understanding cellular function and regulation. Protein acetylation is a common post-translational modification that affects protein activity, localization, and interaction with other proteins. By analyzing the acetylation status of proteins in combination with proteomics or metabolomics, researchers can gain a more complete picture of cellular signaling pathways and metabolic processes. The integration of acetylation modification analysis with other -omics techniques has already yielded important insights into disease mechanisms and has the potential to identify novel therapeutic targets. For example, the dysregulation of protein acetylation has been implicated in a variety of diseases, including cancer and neurodegenerative disorders. Ultimately, the combination of acetylation modification analysis with other -omics techniques will play a key role in advancing our understanding of cellular function and in the development of new diagnostic and therapeutic approaches.

Case 1 Identification of Fungal-Induced Protein Hyperacetylation in Maize Using Acetylome Profiling (1)

Acetylation is an important post-translational modification, and numerous studies have demonstrated the crucial role of histone acetylation in plant defense. The interaction between pathogens and plants is a key scientific question in plant immunity. Cochliobolus carbonum race 1, a fungal pathogen of maize, enhances its ability to infect maize plants by producing HC-toxin (HCT). To further understand how HCT promotes fungal virulence and suppresses plant immunity, a research team from the University of California used proteomics and acetylomics to investigate the acetylation of histones and non-histone proteins in plants exposed to HCT.

The authors analyzed the proteome and acetylome (lysine) of experimental and control groups using mass spectrometry. The results revealed the quantification of 3,636 proteins in the proteome and 912 proteins and 2,791 acetylation sites in the acetylome. By selecting differentially expressed proteins, 171 upregulated and 116 downregulated proteins were identified. The differentially expressed proteins were significantly enriched in the tryptophan biosynthesis pathway.

All detected proteins related to each step in tryptophan biosynthesis are shown(1).

Subsequently, differentially acetylated proteins were selected for analysis, revealing that HCT not only altered the acetylation of histones but also non-histone proteins.

The results of this study suggest that acetylation modification in maize is widespread, and that HCT can regulate plant enzyme activity to alter the levels of protein acetylation modification during the immune response process. Furthermore, in the interaction between the pathogen and the plant, Cochliobolus carbonum race 1 may utilize HCT to reprogram the transcription of infection-related genes in plants, leading to ineffective defense responses.

Case 2 Maximal Exercise Capacity Linked to Muscle Fuel Selection and Mitochondrial Protein Acetylation Changes (2)

During exercise, the body's main sources of fuel come from three types, with the majority coming from fatty acids and carbohydrates, and a small amount coming from amino acids. In order to compare exercise capacity and fuel selection, as well as subsequent metabolic changes, researchers used metabolomics analysis to measure the changes in metabolite levels of LCR and HCR rats at different exercise times, including blood glucose, muscle glycogen, plasma fatty acids, acylcarnitines, amino acids, and plasma branched-chain ketoacids, followed by differential metabolite screening.

After analyzing the metabolomics data, the researchers then sought to find changes in the relevant proteins in these metabolic pathways. The researchers extracted mitochondria from rat muscles and quantitatively analyzed their protein, phosphorylation modification, and acetylation modification changes. The experiment identified 428 mitochondrial proteins, of which 73 were phosphorylated and 85 were acetylated. The results showed that there was no significant difference in protein expression levels and phosphorylation modification between animals with different exercise capacity, but there was a significant difference in acetylation modification levels. Subsequently, further analysis was carried out on the acetylation differential proteins.

Mitochondrial Protein Acetylation Is Dynamic with Exercise (2)

Using proteomics (proteome, phosphorylation modification, acetylation modification) analysis, the results revealed that the acetylation modification of proteins in metabolic pathways (such as BCAA and FA metabolism) may play an important role in exercise capacity. Analysis of changes in metabolites in the BCAA degradation pathway was performed. The use of isotope tracer flux analysis of valine confirmed that protein deacetylation during exercise was accompanied by an increase in BCAA degradation and metabolism.


  1. Walley, Justin W., et al. "Fungal-induced protein hyperacetylation in maize identified by acetylome profiling." Proceedings of the National Academy of Sciences 115.1 (2018): 210-215.
  2. Overmyer, Katherine A., et al. "Maximal oxidative capacity during exercise is associated with skeletal muscle fuel selection and dynamic changes in mitochondrial protein acetylation." Cell metabolism 21.3 (2015): 468-478.
* For Research Use Only. Not for use in diagnostic procedures.
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