GO:0006473 protein acetylation: Mechanism, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0006473 (protein acetylation) describes the enzymatic addition of an acetyl group (CH3CO-) to a protein amino acid, a reversible post-translational modification conserved from bacteria to humans.
• Acetylation is catalyzed by acetyltransferases using acetyl coenzyme A (acetyl-CoA) as the acetyl donor, and removed by deacetylases; the balance between these enzymes controls protein function.
• Protein acetylation regulates enzyme activity, protein stability, subcellular localization, protein-protein interactions, and DNA-binding of transcription factors.
• In bacteria, acetylation is a major regulatory modification influencing metabolism and virulence, and is studied with mass-spectrometry-based acetylome methods.
• In eukaryotes, acetylation occurs in the nucleus, cytoplasm, mitochondria, and peroxisomes, and is tightly linked to acetyl-CoA metabolism.
• Dysregulated acetylation is implicated in cancer, metabolic disease, and neurodegeneration, making acetylation enzymes and reader domains important experimental targets.
Description
Protein acetylation (GO:0006473) is a post-translational modification in which an acetyl group, CH3CO-, is covalently added to a protein amino acid. It is one of the most widespread and evolutionarily conserved protein modifications, occurring in bacteria, plants, yeast, and humans. Because acetylation can change a protein's charge, conformation, and interaction surface, it serves as a rapid and reversible switch that cells use to control enzyme activity, localization, and stability. Researchers study protein acetylation to understand how metabolic states are translated into protein-level regulation and how this process goes wrong in disease. The modification is written and erased by opposing enzyme families: acetyltransferases transfer the acetyl group from acetyl coenzyme A (acetyl-CoA) onto substrate lysine residues, while deacetylases remove it. This dynamic cycle allows acetylation to act as a metabolic sensor, since acetyl-CoA availability directly influences the extent of modification. In bacteria, acetylation regulates central metabolism, stress responses, and virulence, and has become a model system for understanding non-histone acetylation. In eukaryotes, acetylation controls nuclear transcription factors, mitochondrial metabolic enzymes, and peroxisomal proteins, linking the modification to diverse cellular functions. Because acetylation is reversible and enzyme-controlled, it is an attractive target for experimental manipulation using CRISPR-based models and for therapeutic exploration.
protein acetylation At A Glance
| GO ID | GO:0006473 |
|---|---|
| GO term | protein acetylation |
| Ontology | biological_process |
| Synonym | protein amino acid acetylation |
| Definition | The addition of an acetyl group to a protein amino acid; the acetyl group is CH3CO-, derived from acetic (ethanoic) acid. |
| Major function | Reversible post-translational modification that regulates protein activity, stability, localization, and interactions. |
| Acetyl donor | Acetyl coenzyme A (acetyl-CoA). |
| Opposing enzymes | Acetyltransferases (writers) and deacetylases (erasers). |
| Conservation | Occurs in bacteria, plants, yeast, and humans. |
| Subcellular sites | Nucleus, cytoplasm, mitochondria, and peroxisomes. |
| Research methods | Mass spectrometry acetylome profiling, immunoblotting with anti-acetyl-lysine antibodies, and genetic perturbation. |
What Is GO:0006473?
According to the Gene Ontology, GO:0006473 (protein acetylation) is defined as the addition of an acetyl group to a protein amino acid, where the acetyl group is CH3CO-, derived from acetic (ethanoic) acid. In practical terms, it is the enzymatic transfer of an acetyl moiety onto a residue of a target protein, most commonly the epsilon-amino group of a lysine side chain, forming an N-epsilon-acetyl-lysine. The synonym protein amino acid acetylation reflects this broad residue-level definition. The process is a biological process (ontology aspect: biological_process) and is distinct from histone acetylation as a chromatin-specific term, although histone acetylation is a subtype of protein acetylation. Protein acetylation is reversible and depends on the opposing activities of acetyltransferases and deacetylases, with acetyl-CoA serving as the acetyl donor.
Why Is protein acetylation Important in Cell Biology?
Protein acetylation is important because it converts metabolic and environmental signals into rapid changes in protein function without altering protein abundance. Because acetyl-CoA is both a central metabolic intermediate and the acetyl donor for acetylation, the modification directly couples cellular metabolism to the regulation of enzymes, transcription factors, and structural proteins. In bacteria, acetylation controls virulence programs and metabolic enzymes, making it relevant to infectious disease research. In eukaryotes, acetylation regulates nuclear gene expression, mitochondrial energy metabolism, and peroxisomal functions, so its perturbation affects growth, stress responses, and cell survival. Consequently, mapping acetylation sites and identifying the enzymes that write and erase them is a major goal in functional genomics and drug discovery.
• Acetylation is a reversible post-translational modification that regulates protein activity without changing protein levels.
• It uses acetyl-CoA as the acetyl donor, directly linking protein regulation to cellular metabolism.
• Acetyltransferases and deacetylases form opposing enzyme pairs that set the acetylation state of substrates.
• In bacteria, acetylation influences central metabolism, stress responses, and virulence.
• In eukaryotes, acetylation controls transcription factors, metabolic enzymes, and mitochondrial function.
• Plant peroxisomal proteins are also acetylated, showing the modification is conserved beyond animals and microbes.
• Acetylation can alter protein stability, localization, and protein-protein interactions.
• Dysregulated acetylation is associated with cancer and metabolic disorders, motivating therapeutic interest.
• Mass spectrometry-based acetylome studies have revealed hundreds to thousands of acetylation sites across species.
• CRISPR-based knockout and knock-in models allow causal testing of acetylation enzymes and acceptor sites.
What Happens During protein acetylation?
Acetyl-CoA supply and metabolic sensing
In simple terms: The cell first needs a supply of acetyl groups, which come from a central metabolic molecule called acetyl-CoA.
Protein acetylation depends on acetyl coenzyme A (acetyl-CoA), which serves as the acetyl donor for the modification. Because acetyl-CoA is a central metabolite produced by carbohydrate, fat, and amino acid metabolism, its availability directly influences how much acetylation can occur. In budding yeast, changes in acetyl-CoA metabolism alter the acetylation state of many proteins, establishing acetylation as a metabolic sensor. In mitochondria, acetyl-CoA pools and acetylation are closely coupled, so mitochondrial metabolic flux can shape the mitochondrial acetylome. This step is therefore the metabolic entry point for protein acetylation.
Enzymatic transfer of the acetyl group
In simple terms: An enzyme called an acetyltransferase takes the acetyl group from acetyl-CoA and attaches it to a target protein.
Acetyltransferases catalyze the transfer of an acetyl group from acetyl-CoA to a protein amino acid, most commonly the epsilon-amino group of a lysine residue. This produces an N-epsilon-acetyl-lysine and releases coenzyme A. In bacteria, both enzymatic acetylation by acetyltransferases and non-enzymatic acetylation by acetyl-phosphate or acetyl-CoA have been described, expanding the routes to protein acetylation. The GCN5 and PCAF acetyltransferases are evolutionarily conserved enzymes that acetylate non-histone proteins, illustrating that acetylation extends well beyond histones. The reaction is reversible, which is essential for acetylation to act as a regulatory switch.
Substrate recognition and site specificity
In simple terms: Different acetyltransferases choose different target proteins and different positions on those proteins.
Acetyltransferases do not modify all proteins equally; they recognize specific substrate sequences and structural features, leading to defined acetylation sites. Mass spectrometry-based acetylome studies have mapped acetylation to diverse proteins, including metabolic enzymes, ribosomal proteins, and transcription factors. In bacteria, acetylation sites are distributed across central metabolic enzymes and virulence regulators, indicating broad substrate range with context-dependent specificity. In eukaryotes, GCN5 and PCAF acetylate distinct non-histone substrates, showing that substrate selection is enzyme-dependent. Site specificity is a major determinant of the functional consequence of acetylation.
Deacetylation and reversibility
In simple terms: Another set of enzymes, deacetylases, removes the acetyl group so the modification can be turned off.
Deacetylases remove acetyl groups from modified proteins, reversing the modification and allowing dynamic regulation. The balance between acetyltransferase and deacetylase activity determines the steady-state acetylation level of a given protein. In bacteria, deacetylases such as sirtuin-family enzymes contribute to acetylation dynamics and metabolic regulation. In eukaryotes, deacetylation is required for resetting regulatory circuits and for responding to changing metabolic conditions. Reversibility is the property that makes acetylation suitable for rapid signaling.
Functional consequences for the modified protein
In simple terms: Once acetylated, a protein can change its activity, stability, location, or binding partners.
Acetylation can alter enzyme catalytic activity, protein stability, subcellular localization, and protein-protein interactions. In mitochondria, acetylation of metabolic enzymes modulates flux through oxidative phosphorylation and related pathways. In bacteria, acetylation of virulence regulators changes their DNA-binding and regulatory output, linking acetylation to infection. In plants, acetylation of peroxisomal proteins suggests roles in peroxisomal metabolism and stress responses. These downstream effects explain why protein acetylation is studied across microbiology, plant biology, and human disease research.
Key Genes Involved in GO:0006473 protein acetylation
The following genes and proteins are central to the study of protein acetylation, spanning acetyltransferases, deacetylases, metabolic enzymes, and regulatory factors described in the verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| GCN5 (KAT2A) | Conserved acetyltransferase that acetylates non-histone proteins | Model enzyme for studying substrate specificity and non-histone acetylation |
| PCAF (KAT2B) | Conserved acetyltransferase acting on non-histone substrates | Comparative studies of acetyltransferase function and redundancy |
| SIRT family deacetylases | Remove acetyl groups and contribute to acetylation dynamics | Study of reversibility and metabolic regulation of acetylation |
| Acetyl-CoA metabolic enzymes | Supply or consume acetyl-CoA, influencing acetylation | Link between metabolism and protein acetylation in yeast |
| Bacterial acetyltransferases | Enzymatic acetylation of bacterial proteins | Mechanistic studies of bacterial acetylation and virulence |
| Bacterial virulence regulators | Acetylation alters regulatory activity during infection | Host-pathogen interaction and virulence regulation studies |
| Mitochondrial metabolic enzymes | Acetylation modulates mitochondrial flux | Mitochondrial acetylome and metabolic disease research |
| Peroxisomal proteins | Acetylation of plant peroxisomal proteins | Plant peroxisomal biology and stress response studies |
| Ribosomal proteins | Acetylation detected in acetylome studies | Functional analysis of translation-related acetylation |
| Transcription factors | Acetylation affects DNA binding and activity | Gene regulation and chromatin-adjacent acetylation studies |
| Stress response proteins | Acetylation participates in stress signaling | Microbial stress and adaptation research |
| Central metabolic enzymes | Acetylation regulates enzymatic activity | Metabolic flux and acetylome profiling |
| Sirtuin substrates | Deacetylation targets in bacteria and eukaryotes | Reversibility and aging-related acetylation research |
| Acetyl-phosphate-related pathways | Non-enzymatic acetylation routes in bacteria | Chemical biology of acetylation |
| Acetyl-lysine reader domains | Interpret acetylation marks | Functional dissection of acetylation signaling |
| Peroxisomal metabolic enzymes | Acetylation in plant peroxisomes | Plant cell biology and organelle acetylation |
How Is protein acetylation Regulated?
Protein acetylation is regulated at multiple levels. The availability of acetyl-CoA, the acetyl donor, directly controls the extent of modification, linking acetylation to central metabolism. In budding yeast, perturbations in acetyl-CoA metabolism change the acetylation state of many proteins, demonstrating metabolic control of the acetylome. In mitochondria, acetylation is coupled to mitochondrial metabolic flux and acetyl-CoA pools, so changes in energy metabolism reshape the mitochondrial acetylome. The opposing activities of acetyltransferases and deacetylases set steady-state acetylation levels, and altering either enzyme class shifts the balance. In bacteria, acetylation is influenced by both enzymatic and non-enzymatic routes, including acetyl-phosphate-dependent mechanisms, adding a chemical layer of regulation. Substrate recognition by acetyltransferases provides another regulatory layer, since only specific proteins and sites are modified under given conditions. Together, these mechanisms allow protein acetylation to respond dynamically to metabolic and environmental signals.
protein acetylation and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| GCN5 (KAT2A) | Cancer-related gene regulation through non-histone acetylation | Knockout and point-mutation cell models to test substrate-specific effects |
| PCAF (KAT2B) | Cancer and transcriptional regulation via non-histone acetylation | Knockout and overexpression models for comparative acetyltransferase studies |
| Mitochondrial metabolic enzymes | Metabolic and mitochondrial dysfunction linked to acetylation | Knock-in of acetylation-site mutations to test metabolic flux |
| Bacterial virulence regulators | Bacterial virulence and infection | Bacterial knockout and acetylation-site mutant strains |
| Peroxisomal proteins | Plant peroxisomal metabolism and stress responses | Plant knockout and tagged knock-in lines for acetylation mapping |
Protein acetylation in cancer
Dysregulated protein acetylation is implicated in cancer through altered activity of acetyltransferases and deacetylases that control transcription factors and metabolic enzymes. The conserved GCN5 and PCAF acetyltransferases acetylate non-histone proteins involved in gene regulation, and their dysfunction can perturb proliferative and metabolic programs. Because acetylation is reversible, enzymes that write and erase the mark are considered candidate therapeutic targets. Experimental models that knockout or mutate acetylation enzymes help determine whether a specific acetylation event is causal in tumor biology.
Protein acetylation in metabolic and mitochondrial disease
Mitochondrial protein acetylation is tightly linked to metabolic flux, and altered acetylation of mitochondrial enzymes can affect energy production. Because acetyl-CoA availability controls acetylation, metabolic disorders that change acetyl-CoA pools may indirectly reshape the mitochondrial acetylome. In yeast, acetyl-CoA metabolism directly influences protein acetylation, providing a model for how metabolic state and acetylation are coupled. These connections make acetylation enzymes and sites relevant to metabolic disease research.
Protein acetylation in bacterial virulence and infection
In bacteria, protein acetylation regulates virulence programs, and acetylation of virulence regulators can change their activity during infection. Bacterial acetylation is studied both as a basic regulatory mechanism and as a potential target for anti-virulence strategies. Because acetylation affects central metabolic enzymes and stress responses, it contributes to bacterial adaptation within the host. Understanding which bacterial proteins are acetylated and by which enzymes is therefore important for infection biology.
Protein acetylation in plant peroxisomal biology
Protein acetylation has been identified as a post-translational modification of plant peroxisomal proteins, expanding the known roles of acetylation beyond animals and microbes. This finding suggests that acetylation may regulate peroxisomal metabolism and stress responses in plants. Studying plant peroxisomal acetylation provides comparative insight into the evolution and function of the modification. It also highlights that acetylation research requires organism-specific models.
From protein acetylation-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is an acetyltransferase required for a specific acetylation event? | Knockout cell model of the acetyltransferase gene |
| Does a single acetylation site control protein function? | Point-mutation knock-in of the acceptor residue |
| Where and when is an acetylated protein localized? | Tagged knock-in with an epitope or fluorescent tag |
| Does increased acetylation change phenotype? | Overexpression of the acetyltransferase or a deacetylase-deficient background |
| Which proteins are acetylated under a given condition? | Acetylome profiling by mass spectrometry in wild-type and mutant cells |
| Is acetylation conserved across species? | Comparative knockout and acetylome analysis in bacterial, yeast, and plant models |
How to Study the protein acetylation Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Mass spectrometry acetylome profiling | Acetylated peptides and sites across the proteome | Global mapping of acetylation in cells and tissues |
| Anti-acetyl-lysine immunoblotting | Acetylation level of specific proteins | Validation of acetylation changes after perturbation |
| Immunoprecipitation | Acetylated protein complexes | Enrichment of acetylated proteins for downstream analysis |
| Genetic knockout of acetyltransferases | Requirement of an enzyme for acetylation | Assigning enzyme-substrate relationships |
| Deacetylase inhibition or knockout | Effect of removing the eraser enzyme | Testing reversibility and steady-state acetylation |
| Acetyl-CoA measurement | Availability of the acetyl donor | Linking metabolism to acetylation state |
| Site-directed mutagenesis | Function of a specific acetylation site | Testing causality of individual acetylation events |
| Comparative acetylome analysis | Conservation of acetylation across species | Evolutionary and organism-specific studies |
Mass spectrometry-based acetylome profiling
Mass spectrometry is the primary method for mapping protein acetylation sites across a proteome. Acetyl-lysine enrichment followed by liquid chromatography-tandem mass spectrometry identifies modified peptides and their sites. This approach has revealed hundreds to thousands of acetylation sites in bacteria, yeast, and other organisms. Comparative acetylome profiling between wild-type and mutant strains can link specific enzymes to specific sites.
Antibody-based detection of acetylation
Anti-acetyl-lysine antibodies allow detection of acetylation on specific proteins by immunoblotting or immunoprecipitation. These reagents are useful for validating mass spectrometry findings and for monitoring acetylation changes after genetic or metabolic perturbation. Antibody-based methods are widely used in bacterial and eukaryotic acetylation studies.
Genetic perturbation of acetylation enzymes
Knockout, knockdown, or overexpression of acetyltransferases and deacetylases is used to test causality between an enzyme and an acetylation event. In yeast, manipulation of acetyl-CoA metabolism combined with genetic perturbation reveals how metabolism controls acetylation. In bacteria, deletion of acetyltransferase genes helps assign enzyme-substrate relationships. These approaches are complementary to global acetylome profiling.
Metabolic and acetyl-CoA measurements
Because acetyl-CoA is the acetyl donor, measuring acetyl-CoA levels helps interpret acetylation changes. In mitochondria, acetyl-CoA pools are linked to the mitochondrial acetylome, so metabolic flux measurements complement acetylation data. In yeast, acetyl-CoA metabolism is directly connected to protein acetylation, making metabolite measurement an important part of acetylation research. Combining metabolomics with acetylome profiling provides a systems-level view.
How CRISPR Can Be Used to Study GO:0006473 protein acetylation
Knockout
CRISPR knockout of acetyltransferase or deacetylase genes is used to test whether an enzyme is required for a specific acetylation event or phenotype. In bacteria, gene deletion combined with acetylome profiling assigns enzyme-substrate relationships. In yeast, knockout of metabolic genes that control acetyl-CoA helps dissect the link between metabolism and acetylation. Knockout models are therefore a first-line approach for causal testing in protein acetylation research.
Point Mutation
CRISPR point mutation can substitute the acceptor lysine residue of a target protein to a non-acetylatable residue, allowing direct testing of a single acetylation site. This approach is valuable when a protein has multiple acetylation sites and the goal is to separate their functions. Point-mutation models complement enzyme knockouts by isolating the consequence of one modification event. They are widely applicable to mitochondrial and nuclear acetylation targets.
Knock-in
CRISPR knock-in can introduce epitope or fluorescent tags at endogenous acetylation-related genes to track protein localization and interactions. Tagged knock-in preserves endogenous regulatory context, which is important because acetylation is dynamic and context-dependent. Knock-in of acetylation-mimicking or acetylation-deficient alleles can also be used to probe function. These models are useful for imaging and proteomic studies of acetylated proteins.
Overexpression
CRISPR-mediated overexpression or cDNA-based overexpression of acetyltransferases and deacetylases is used to test whether increased enzyme dosage changes acetylation and phenotype. Overexpression of GCN5 or PCAF can reveal substrate preferences and downstream effects on non-histone proteins. In metabolic studies, overexpression of acetyl-CoA-related enzymes can shift acetylation states. Overexpression models are complementary to loss-of-function approaches.
How EDITGENE Supports protein acetylation Research
Researchers studying protein acetylation-related genes often need to determine whether a candidate gene is causally involved in a specific acetylation event, whether a single acceptor site mediates a phenotype, and how the modification behaves in a physiologically relevant cell model. Answering these questions requires precise genetic tools that can remove, modify, tag, or overexpress the genes and sites of interest without confounding off-target effects. EDITGENE provides these tools across cell types and species, enabling functional dissection of protein acetylation from enzyme discovery to site-level causality.
Contact EDITGENE today to design your custom CRISPR model for protein acetylation research.
Related Products
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| KAT2B Knockout HEK293 Cell Line | EDJ-KQ429 | Human | 8850 | Details Get a Quote |
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| CLOCK Knockout HeLa Cell Line | EDJ-KQ20020 | Human | 9575 | Details Get a Quote |
| SPHK1 Knockout A-549 Cell Line | EDJ-KQ20196 | Human | 8877 | Details Get a Quote |
| SPHK1 Knockout HCT 116 Cell Line | EDJ-KQ20197 | Human | 8877 | Details Get a Quote |
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Frequently Asked Questions About protein acetylation
What is protein acetylation (GO:0006473)?
Protein acetylation is the addition of an acetyl group (CH3CO-) to a protein amino acid, as defined by the Gene Ontology term GO:0006473. It is a reversible post-translational modification that can change protein activity, stability, localization, and interactions.
What genes are involved in protein acetylation?
Key genes include acetyltransferases such as GCN5 and PCAF, deacetylases such as the sirtuin family, and metabolic genes that control acetyl-CoA availability. Bacterial acetyltransferases and virulence regulators are also central to acetylation research in microbes.
What is the difference between protein acetylation and histone acetylation?
Protein acetylation (GO:0006473) is the broad term for acetyl addition to any protein amino acid, while histone acetylation is a chromatin-specific subtype. Non-histone acetylation by GCN5 and PCAF shows that the modification extends well beyond histones.
How is protein acetylation regulated?
It is regulated by the balance between acetyltransferases and deacetylases, and by the availability of acetyl-CoA, the acetyl donor. In mitochondria and yeast, metabolic flux and acetyl-CoA pools directly influence acetylation state.
Why is protein acetylation important in bacteria?
Bacterial protein acetylation regulates central metabolism, stress responses, and virulence, and can occur through both enzymatic and non-enzymatic routes. It is studied as a model for non-histone acetylation and as a potential anti-virulence target.
What methods are used to study protein acetylation?
Common methods include mass spectrometry-based acetylome profiling, anti-acetyl-lysine immunoblotting, genetic perturbation of acetylation enzymes, and acetyl-CoA measurement. Site-directed mutagenesis is used to test individual acetylation sites.
Is protein acetylation reversible?
Yes, protein acetylation is reversible; deacetylases remove acetyl groups and reset the modification state. This reversibility allows acetylation to act as a dynamic regulatory switch.
What is the role of acetyl-CoA in protein acetylation?
Acetyl-CoA is the acetyl donor for protein acetylation, so its availability directly controls the extent of modification. In yeast and mitochondria, acetyl-CoA metabolism is tightly coupled to the acetylation state of many proteins.
Can CRISPR be used to study protein acetylation?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models can test the causal role of acetylation enzymes and acceptor sites. These models complement mass spectrometry-based acetylome profiling.
Is protein acetylation conserved across species?
Protein acetylation is conserved from bacteria to plants, yeast, and humans, although the specific substrates and enzymes differ. Comparative acetylome studies help reveal conserved and species-specific acetylation events.
Conclusion
Protein acetylation (GO:0006473) is a conserved, reversible post-translational modification that links acetyl-CoA metabolism to the regulation of protein activity, stability, localization, and interactions. It is catalyzed by acetyltransferases and reversed by deacetylases, and it occurs in bacteria, plants, yeast, and humans. Because acetylation influences virulence, mitochondrial metabolism, peroxisomal function, and transcription, it is relevant to infection biology, metabolic disease, cancer, and plant biology. Continued progress depends on precise genetic models and global acetylome profiling to assign enzymes to sites and to test causality. CRISPR-based knockout, point-mutation, knock-in, and overexpression models, combined with mass spectrometry and bioinformatics, provide the experimental framework needed to move from correlation to mechanism in protein acetylation research.
References
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- 2. Jones JD et al.. 2011. Protein acetylation in prokaryotes.. Proteomics 11(15):3012-22 PMID: 21674803
- 3. Reumann S et al.. 2025. Protein acetylation as a novel post-translational modification of plant peroxisomal proteins.. J Exp Bot 76(12):3311-3323 PMID: 40290089
- 4. Ren J et al.. 2017. Protein Acetylation and Its Role in Bacterial Virulence.. Trends Microbiol 25(9):768-779 PMID: 28462789
- 5. Downey M. 2021. Non-histone protein acetylation by the evolutionarily conserved GCN5 and PCAF acetyltransferases.. Biochim Biophys Acta Gene Regul Mech 1864(2):194608 PMID: 32711095
- 6. Wolfe AJ. 2016. Bacterial protein acetylation: new discoveries unanswered questions.. Curr Genet 62(2):335-41 PMID: 26660885
- 7. Baeza J et al.. 2016. Mechanisms and Dynamics of Protein Acetylation in Mitochondria.. Trends Biochem Sci 41(3):231-244 PMID: 26822488
- 8. Galdieri L et al.. 2014. Protein acetylation and acetyl coenzyme a metabolism in budding yeast.. Eukaryot Cell 13(12):1472-83 PMID: 25326522
