GO:0004596 protein-N-terminal amino-acid acetyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004596 describes the enzymatic activity that transfers an acetyl group from acetyl-CoA to the N-terminal amino acid of a protein, a co-translational modification known as N-terminal acetylation [1,4].
• This activity is carried out by N-terminal acetyltransferase (NAT) complexes, which in humans include NatA, NatB, NatC, NatD, NatE, and NatF, each with distinct substrate specificities [1,6].
• N-terminal acetylation influences protein stability, localization, and interactions, and is implicated in cancer, developmental disorders, and neurodegeneration [1,3,5,6].
• Key catalytic subunits include NAA10, NAA20, NAA30, NAA40, NAA50, and NAA60, which are being actively studied as potential drug targets [2,6,8].
• Dysregulation of NAT activity can affect mitochondrial degradation, amyloid-beta secretion, and cell proliferation, linking the enzyme to diverse disease pathways [3,5].
• CRISPR-based knockout, point mutation, knock-in, and overexpression models are essential tools for dissecting the precise roles of individual NAT subunits in health and disease [1,6].
Description
Protein N-terminal acetylation is one of the most abundant protein modifications in eukaryotes, affecting roughly 80% of cytosolic proteins. The enzyme activity responsible for this modification, classified as GO:0004596 (protein-N-terminal amino-acid acetyltransferase activity), catalyzes the transfer of an acetyl group from acetyl-CoA to the alpha-amino group of the first amino acid of a nascent polypeptide [1,4]. This modification is irreversible and occurs co-translationally, influencing protein folding, stability, and interactions. The importance of this activity is underscored by its evolutionary conservation from yeast to humans and its involvement in a wide range of cellular processes [1,7]. Research over the past two decades has revealed that N-terminal acetyltransferases (NATs) are not merely housekeeping enzymes but key regulators of protein function. The human genome encodes several NAT complexes, each with distinct substrate specificities and biological roles [1,6]. For example, the NatA complex, which acetylates proteins with small N-terminal residues after methionine excision, is critical for selective mitochondrial degradation. The NatB complex, which acetylates proteins with N-terminal methionine followed by acidic residues, has been linked to developmental delay and intellectual disability when mutated. These findings highlight the physiological significance of GO:0004596 and its potential as a therapeutic target. Given the broad impact of N-terminal acetylation, understanding the molecular mechanisms, regulation, and disease associations of this activity is essential for researchers in cell biology, genetics, and drug discovery. This article provides a comprehensive overview of GO:0004596, covering its definition, catalytic mechanism, key genes, regulatory pathways, disease implications, and state-of-the-art research methods including CRISPR-based models.
protein-N-terminal amino-acid acetyltransferase activity At A Glance
| GO ID | GO:0004596 |
|---|---|
| GO term | protein-N-terminal amino-acid acetyltransferase activity |
| Ontology | molecular_function |
| Synonym | N(alpha)-acetyltransferase activity; NAT activity; peptide alpha-N-acetyltransferase activity; protein N-terminal acetyltransferase activity |
| Major function | Catalyzes the co-translational transfer of an acetyl group from acetyl-CoA to the N-terminal amino acid of a protein, influencing protein stability, localization, and interactions. |
| Reaction | acetyl-CoA + an N-terminal L-alpha-aminoacyl-[protein] = CoA + H+ + N-terminal Nalpha-acetyl-L-alpha-aminoacyl-[protein] |
| Substrates | Acetyl-CoA and proteins with diverse N-terminal sequences (e.g., Ser-, Ala-, Met-, Gly-). |
| Localization | Cytosol, nucleus, mitochondria, and ribosome-associated complexes. |
| Enzyme family | N-terminal acetyltransferases (NATs), including NatA, NatB, NatC, NatD, NatE, NatF. |
What Is GO:0004596?
GO:0004596, protein-N-terminal amino-acid acetyltransferase activity, is defined as the catalysis of the reaction: acetyl-CoA + an N-terminal L-alpha-aminoacyl-[protein] = CoA + H+ + N-terminal Nalpha-acetyl-L-alpha-aminoacyl-[protein]. In simpler terms, it is the enzyme activity that attaches an acetyl group to the very first amino acid of a protein, using acetyl-CoA as the acetyl donor. This modification is also known as N-alpha-acetylation or N-terminal acetylation and is distinct from lysine acetylation on internal residues. The activity is carried out by a family of enzymes called N-terminal acetyltransferases (NATs), which recognize specific N-terminal sequences and catalyze the transfer of the acetyl group to the alpha-amino group of the N-terminal residue [1,4].
Why Is protein-N-terminal amino-acid acetyltransferase activity Important in Cell Biology?
GO:0004596 is fundamental to proteostasis because N-terminal acetylation affects nearly all aspects of protein life cycle, from folding and stability to subcellular targeting and protein-protein interactions. Dysregulation of this activity has been directly linked to cancer, developmental disorders, and neurodegeneration, making it a focal point for both basic research and therapeutic development [1,3,5,6]. Understanding the precise molecular mechanisms and substrate specificities of NATs is therefore critical for deciphering disease pathways and for designing targeted interventions.
• N-terminal acetylation is one of the most common protein modifications in eukaryotes, affecting ~80% of cytosolic proteins.
• It regulates protein stability by creating degrons (e.g., Ac/N-degron) that are recognized by E3 ubiquitin ligases.
• NAT complexes are essential for normal development; mutations in NAA20 cause autosomal recessive developmental delay, intellectual disability, and microcephaly.
• The activity influences amyloid precursor protein processing and Aβ secretion, linking it to Alzheimer's disease.
• NATs are overexpressed in various cancers and represent potential anticancer targets [1,2].
• N-terminal acetylation affects mitochondrial function and selective degradation of mitochondrial proteins.
• The catalytic mechanism of hNaa50p follows an ordered sequential mechanism, providing a framework for inhibitor design.
• Yeast genetics has been instrumental in identifying NAT genes and their substrates, revealing conserved functions.
• Human NAA10 and its duplicate NAA11 (hARD2) exhibit distinct tissue-specific expression and substrate preferences.
• Small-molecule inhibitors of NATs, such as bisubstrate inhibitors for NAA40, are being developed as research tools and therapeutics.
Molecular Mechanism of protein-N-terminal amino-acid acetyltransferase activity
Substrate Recognition and Binding
In simple terms: The enzyme first grabs the target protein and the acetyl donor, positioning them for the reaction.
N-terminal acetyltransferases (NATs) recognize specific N-terminal sequences of nascent polypeptides as they emerge from the ribosome. For example, NatA prefers N-terminal Ser, Ala, Thr, Val, or Gly after methionine excision, while NatB acts on Met-Asp or Met-Glu starts [1,6]. The enzyme binds acetyl-CoA and the protein substrate in an ordered manner, as demonstrated for human hNaa50p (hNAT5/hSAN), which follows an ordered sequential catalytic mechanism where acetyl-CoA binds first, followed by the peptide substrate. This precise recognition ensures that only proteins with appropriate N-termini are acetylated.
Catalytic Transfer of the Acetyl Group
In simple terms: The enzyme transfers the acetyl group from acetyl-CoA to the protein's front end.
Once both substrates are bound, the catalytic subunit of the NAT complex catalyzes the transfer of the acetyl group from acetyl-CoA to the alpha-amino group of the N-terminal amino acid. This reaction releases CoA and H+ and results in an N-alpha-acetylated protein. The catalytic mechanism involves general acid-base catalysis, with conserved residues in the NAT domain facilitating the nucleophilic attack of the N-terminal amino group on the acetyl-CoA thioester. Kinetic and NMR studies on hNaa50p have provided detailed insights into this ordered sequential mechanism, revealing conformational changes that accompany substrate binding and catalysis.
Co-translational Nature and Ribosome Association
In simple terms: The modification happens while the protein is still being made on the ribosome.
N-terminal acetylation predominantly occurs co-translationally, meaning the acetyl group is added while the nascent polypeptide chain is still attached to the ribosome. This requires NAT complexes to interact with ribosomes, either directly or through accessory proteins. For instance, the NatA complex associates with ribosomes via Naa10 and Naa15, allowing it to act on nascent chains as soon as the N-terminus emerges from the ribosomal exit tunnel [1,5]. This co-translational timing is crucial for the modification's impact on protein folding and stability.
Substrate Specificity and Complex Diversity
In simple terms: Different NAT complexes recognize different starting sequences, allowing a wide range of proteins to be modified.
Humans possess multiple NAT complexes (NatA, NatB, NatC, NatD, NatE, NatF) with distinct substrate specificities determined by the catalytic subunits (e.g., NAA10, NAA20, NAA30, NAA40, NAA50, NAA60) and auxiliary subunits [1,6]. For example, NatD (NAA40) specifically acetylates histone H4 and H2A N-termini, while NatF (NAA60) acts on transmembrane proteins at the Golgi. This diversity allows for selective regulation of different protein subsets. The ordered sequential mechanism observed for hNaa50p may be a common feature among NATs, ensuring efficient catalysis.
Regulation and Post-Translational Control
In simple terms: The activity can be turned up or down by other cellular signals.
NAT activity is regulated at multiple levels, including expression of catalytic and auxiliary subunits, post-translational modifications, and availability of acetyl-CoA. For instance, the NatA complex is regulated by the abundance of its subunits, and its activity is influenced by cellular metabolic status. Additionally, N-terminal acetylation can be reversed? No, it is generally irreversible, but the modification can be outcompeted by other N-terminal modifications such as arginylation or methionine excision [1,5]. Dysregulation of NAT expression is observed in cancer, where NAA10 and NAA20 are often overexpressed [1,6].
Key Genes Involved in GO:0004596 protein-N-terminal amino-acid acetyltransferase activity
The following genes encode catalytic subunits and auxiliary components of N-terminal acetyltransferase complexes that carry out GO:0004596 activity.
| Gene | Major Role | Research Relevance |
|---|---|---|
| NAA10 | Catalytic subunit of NatA; acetylates Ser/Ala/Thr/Val/Gly N-termini | Mutations linked to Ogden syndrome; overexpressed in cancers; essential for mitochondrial degradation [1,5] |
| NAA11 | hARD2, a processed duplicate of NAA10; N-alpha-acetyltransferase | Tissue-specific expression; potential role in cancer and development |
| NAA15 | Auxiliary subunit of NatA; ribosome binding | Required for NatA stability and function; implicated in neurodevelopmental disorders |
| NAA20 | Catalytic subunit of NatB; acetylates Met-Asp/Glu N-termini | Mutations cause developmental delay, intellectual disability, microcephaly |
| NAA25 | Auxiliary subunit of NatB | Essential for NatB complex formation and substrate recognition |
| NAA30 | Catalytic subunit of NatC; acetylates Met-Ile/Leu/Phe N-termini | Involved in protein stability and cancer; potential drug target |
| NAA35 | Auxiliary subunit of NatC | Required for NatC function; linked to ribosome biogenesis |
| NAA38 | Auxiliary subunit of NatC | Stabilizes NatC complex; may have additional roles in translation |
| NAA40 | Catalytic subunit of NatD; acetylates histone H4 and H2A | Specific for histones; bisubstrate inhibitors developed |
| NAA50 | Catalytic subunit of NatE; also associated with NatA | Ordered sequential mechanism; potential target in cancer |
| NAA60 | Catalytic subunit of NatF; acetylates transmembrane proteins | Golgi-localized; role in protein sorting and cancer |
| NAA16 | Auxiliary subunit of NatA in higher eukaryotes | Modulates NatA substrate specificity; may affect development |
| NAA80 | Catalytic subunit of NatH; acetylates actin | Regulates actin dynamics; linked to cytoskeletal disorders |
| HYPK | Huntingtin-interacting protein K; NatA auxiliary factor | Enhances NatA activity; may link to neurodegeneration |
| ARD1 | Yeast homolog of NAA10 | Model for studying NAT function and essentiality |
| NAT1 | Yeast NAA15 homolog | Auxiliary subunit in yeast NatA; genetic studies |
| MAK10 | Yeast NAA35 homolog | NatC auxiliary subunit; mitochondrial degradation |
| MAK31 | Yeast NAA38 homolog | NatC auxiliary subunit; mitochondrial degradation |
How Is protein-N-terminal amino-acid acetyltransferase activity Regulated?
N-terminal acetyltransferase activity is regulated at multiple levels. Transcriptional control of catalytic and auxiliary subunits determines the abundance of active NAT complexes. For example, NAA10 and NAA15 are co-regulated to maintain NatA levels. Post-translational modifications, such as phosphorylation, can modulate NAT activity or complex assembly. The availability of acetyl-CoA, a central metabolic intermediate, directly influences the rate of acetylation, linking NAT activity to cellular metabolic state. Additionally, accessory proteins like HYPK can enhance NatA activity and substrate specificity. In yeast, the NatC complex is regulated by the availability of its subunits Mak10 and Mak31, which are required for selective mitochondrial degradation. Dysregulation of NAT expression is common in cancer, where oncogenic signaling pathways may drive overexpression of NAA10 and NAA20 [1,6].
protein-N-terminal amino-acid acetyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| NAA10 | Ogden syndrome; cancer (overexpression) | Knockout and point mutation in cell lines; xenograft models |
| NAA20 | Autosomal recessive developmental delay, intellectual disability, microcephaly | Patient-derived iPSCs; knock-in of patient mutations in HEK293 |
| NAA40 | Colorectal cancer; histone acetylation | Knockout in HCT116; overexpression in normal colon cells |
| NAA50 | Cancer; cell proliferation | Knockdown and knockout in HeLa; rescue with catalytic mutants |
| APP (interaction) | Alzheimer's disease; Aβ secretion | Overexpression of NAT subunits in APP-expressing cells; Aβ ELISA |
Cancer
Dysregulation of N-terminal acetyltransferases is frequently observed in human cancers. NAA10 (NatA catalytic subunit) is overexpressed in several cancer types, including lung, breast, and colorectal cancers, and its expression correlates with poor prognosis. NAA20 (NatB) is also overexpressed in cancers and promotes cell proliferation. The NatD subunit NAA40 is overexpressed in colorectal cancer and its inhibition reduces tumor growth. These findings suggest that NATs contribute to oncogenesis by acetylating proteins involved in cell cycle progression, apoptosis, and metastasis. Targeting NAT activity with small-molecule inhibitors is an emerging therapeutic strategy [1,2].
Neurodevelopmental Disorders
Mutations in NAA20, encoding the catalytic subunit of NatB, cause autosomal recessive developmental delay, intellectual disability, and microcephaly. This highlights the critical role of N-terminal acetylation in brain development. Similarly, mutations in NAA10 have been linked to Ogden syndrome, a rare X-linked disorder characterized by developmental delay, hypotonia, and cardiac arrhythmia. These disorders underscore the importance of precise N-terminal acetylation for neuronal function and development.
Neurodegeneration
N-terminal acetylation is implicated in neurodegenerative diseases. The interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein (APP) affects Aβ secretion, suggesting a role in Alzheimer's disease pathogenesis. Additionally, the NatA complex is critical for selective mitochondrial degradation, and its dysfunction may contribute to Parkinson's disease and other neurodegenerative conditions. These links make NATs potential targets for neuroprotective therapies.
From protein-N-terminal amino-acid acetyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| What is the effect of NAA10 loss on cell viability? | CRISPR knockout of NAA10 in HeLa or HEK293 cells; cell viability assays |
| How does the NAA20 missense mutation affect NatB activity? | Point mutation knock-in of patient variants in HEK293; immunoprecipitation and acetylation assays |
| Does NAA40 overexpression promote tumor growth? | Knock-in of NAA40 under a strong promoter in colorectal cancer cells; xenograft mouse models |
| What proteins are acetylated by NatA? | Tagged knock-in of NAA10 with FLAG tag; immunoprecipitation and mass spectrometry |
| Can NAA50 inhibitors reduce cancer cell proliferation? | Overexpression of NAA50 in cancer cells; treatment with bisubstrate inhibitors |
| What is the role of NatC in mitochondrial degradation? | Knockout of NAA30 or NAA35 in yeast or mammalian cells; mitochondrial turnover assays |
How to Study the protein-N-terminal amino-acid acetyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Mass spectrometry (TAILS, COFRADIC) | Global N-terminal acetylation status | Identify substrates of specific NATs; quantify changes after knockout |
| Enzyme kinetics (NADH-coupled assay) | Catalytic activity and inhibitor potency | Characterize NAT mechanism; screen for inhibitors |
| NMR spectroscopy | Conformational changes and binding order | Elucidate ordered sequential mechanism |
| Cycloheximide chase | Protein stability | Assess impact of N-terminal acetylation on degradation |
| Fluorescence microscopy | Subcellular localization | Determine effect of acetylation on protein targeting |
| CRISPR knockout screens | Gene essentiality and synthetic lethality | Identify pathways compensating for NAT loss |
| Immunoprecipitation + Western blot | Protein interactions and acetylation levels | Validate specific acetylation events |
| Aβ ELISA | Amyloid-beta secretion | Study NAT role in Alzheimer's disease |
Proteomics and Acetylome Profiling
Mass spectrometry-based proteomics is the primary method to identify N-terminally acetylated proteins and quantify changes in acetylation status upon NAT manipulation. Techniques such as N-terminal COFRADIC or TAILS enrich N-terminal peptides, enabling global mapping of N-terminal acetylation. These methods can reveal substrate specificity of individual NATs and identify novel targets. Quantitative acetylome profiling after CRISPR knockout of a specific NAT subunit can uncover its unique substrates and downstream pathways.
Kinetic and Structural Studies
Enzyme kinetics using purified NAT complexes and synthetic peptide substrates provide insights into catalytic mechanisms, substrate affinity, and inhibitor efficacy. For example, combined kinetic and NMR studies on hNaa50p revealed an ordered sequential mechanism. X-ray crystallography and cryo-EM structures of NAT complexes bound to substrates or inhibitors elucidate the molecular basis of substrate recognition and catalysis. These methods are essential for rational drug design targeting NATs.
Cell-Based Assays for Protein Stability and Localization
N-terminal acetylation affects protein half-life and subcellular localization. Cycloheximide chase assays and pulse-chase labeling can measure stability of specific reporter proteins with or without N-terminal acetylation. Fluorescence microscopy of GFP-tagged proteins can assess localization changes upon NAT knockout or overexpression. These assays help link acetylation to functional outcomes such as mitochondrial degradation or APP processing.
CRISPR Screening and Functional Genomics
Genome-wide CRISPR knockout screens can identify genes that are essential in NAT-mutant backgrounds or that modulate sensitivity to NAT inhibitors. Such screens can uncover synthetic lethal interactions and resistance mechanisms. For example, knocking out NAA10 in cancer cell lines followed by CRISPR screening can reveal pathways that compensate for loss of NatA activity. These functional genomics approaches accelerate target validation and drug discovery [1,2].
How CRISPR Can Be Used to Study GO:0004596 protein-N-terminal amino-acid acetyltransferase activity
Knockout
CRISPR knockout of individual NAT catalytic or auxiliary subunits (e.g., NAA10, NAA20, NAA50) is a powerful approach to study loss-of-function phenotypes. Knockout cell lines can be used to identify substrates that become hypoacetylated, assess changes in protein stability and localization, and evaluate effects on cell proliferation, apoptosis, and stress responses [1,6]. For essential genes like NAA10, inducible knockout systems or conditional alleles may be necessary to avoid lethality. Knockout models are also valuable for validating inhibitor specificity.
Point Mutation
Point mutations identified in patients (e.g., NAA20 missense variants causing developmental delay) can be introduced into cell lines using CRISPR prime editing or homology-directed repair to create isogenic models. These models allow researchers to study the functional impact of specific mutations on NAT activity, substrate specificity, and downstream cellular processes. Point mutation knock-in of catalytic dead variants (e.g., NAA10 catalytic mutant) can distinguish enzymatic activity from scaffolding functions.
Knock-in
Knock-in of epitope tags (e.g., FLAG, HA) or fluorescent proteins (e.g., GFP) at the endogenous locus of NAT subunits enables precise tracking of protein expression, localization, and interactions. Tagged knock-in cell lines are ideal for immunoprecipitation followed by mass spectrometry to identify NAT complex components and substrates. Additionally, knock-in of reporter constructs under the control of NAT promoters can be used to study transcriptional regulation.
Overexpression
Overexpression of wild-type or mutant NAT subunits (e.g., NAA10, NAA40) in cell lines can mimic the overexpression observed in cancers and help identify oncogenic mechanisms. Overexpression models are useful for testing small-molecule inhibitors, as they increase the target enzyme levels and may sensitize cells to inhibition. However, overexpression can also lead to artifacts due to non-physiological levels, so results should be validated with endogenous knock-in or knockout models.
How EDITGENE Supports protein-N-terminal amino-acid acetyltransferase activity Research
Researchers studying protein-N-terminal amino-acid acetyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in a specific cellular process or disease. EDITGENE provides a comprehensive suite of CRISPR-based services to accelerate this research, from generating knockout cell lines to creating precise point mutations and knock-in reporters. Our expert team ensures high-quality, publication-ready models tailored to your experimental needs.
Contact EDITGENE today to design your custom CRISPR model for protein-N-terminal amino-acid acetyltransferase activity research.
Frequently Asked Questions About protein-N-terminal amino-acid acetyltransferase activity
What is protein-N-terminal amino-acid acetyltransferase activity?
It is the enzyme activity (GO:0004596) that transfers an acetyl group from acetyl-CoA to the N-terminal amino acid of a protein, a common co-translational modification [1,4].
What genes are involved in protein-N-terminal amino-acid acetyltransferase activity?
Key genes include NAA10, NAA11, NAA15, NAA20, NAA25, NAA30, NAA35, NAA38, NAA40, NAA50, NAA60, and NAA80, which encode subunits of NAT complexes [1,6,8].
Which diseases are linked to N-terminal acetyltransferase dysfunction?
Dysfunction is linked to cancers (e.g., NAA10, NAA20 overexpression), neurodevelopmental disorders (NAA20 mutations), and neurodegeneration (APP processing, mitochondrial degradation) [1,3,5,6].
How is N-terminal acetylation studied experimentally?
Common methods include mass spectrometry-based acetylome profiling, enzyme kinetics, CRISPR knockout/knock-in models, and cell-based assays for protein stability and localization [1,4,5].
What is the catalytic mechanism of N-terminal acetyltransferases?
NATs typically follow an ordered sequential mechanism where acetyl-CoA binds first, followed by the protein substrate, as shown for hNaa50p.
Can N-terminal acetylation be targeted for cancer therapy?
Yes, small-molecule inhibitors of NATs, such as bisubstrate inhibitors for NAA40, are being developed and show promise in preclinical studies.
What is the role of NatA complex in mitochondria?
The NatA complex is critical for selective mitochondrial degradation, and its loss leads to accumulation of damaged mitochondria.
How does N-terminal acetylation affect protein stability?
N-terminal acetylation can create degrons (Ac/N-degrons) that are recognized by E3 ubiquitin ligases, targeting proteins for degradation.
What are the available CRISPR models for studying NAT genes?
EDITGENE offers knockout, point mutation, knock-in, and overexpression models for all major NAT genes, as well as CRISPR library screening services [1,6].
What is the difference between N-terminal acetylation and lysine acetylation?
N-terminal acetylation occurs on the alpha-amino group of the first amino acid and is generally irreversible, while lysine acetylation occurs on side-chain amino groups of internal lysines and is reversible.
Conclusion
GO:0004596, protein-N-terminal amino-acid acetyltransferase activity, is a fundamental enzymatic activity that shapes the eukaryotic proteome. Through the action of diverse NAT complexes, it regulates protein stability, localization, and interactions, with profound implications for development, cancer, and neurodegeneration. Continued research using advanced CRISPR models and proteomic technologies will further illuminate its mechanistic details and therapeutic potential. EDITGENE is committed to supporting this research with high-quality cell models and screening services.
References
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- 3. Asaumi M et al.. 2005. Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion.. J Biochem 137(2):147-55 PMID: 15749829
- 4. Evjenth RH et al.. 2012. Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study.. J Biol Chem 287(13):10081-10088 PMID: 22311970
- 5. Eiyama A et al.. 2015. Protein N-terminal Acetylation by the NatA Complex Is Critical for Selective Mitochondrial Degradation.. J Biol Chem 290(41):25034-44 PMID: 26296886
- 6. Morrison J et al.. 2021. Missense NAA20 variants impairing the NatB protein N-terminal acetyltransferase cause autosomal recessive developmental delay, intellectual disability, and microcephaly.. Genet Med 23(11):2213-2218 PMID: 34230638
- 7. Mullen JR et al.. 1989. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast.. EMBO J 8(7):2067-75 PMID: 2551674
- 8. Arnesen T et al.. 2006. Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-alpha-acetyltransferase.. BMC Biochem 7:13 PMID: 16638120
