GO:0070127 tRNA aminoacylation for mitochondrial protein translation: Protein Synthesis Pathway, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0070127 describes the synthesis of aminoacyl-tRNA by forming an ester bond between the 3'-hydroxyl group of the most 3' adenosine of tRNA and an amino acid, specifically for use in mitochondrial ribosome-mediated polypeptide synthesis.
• Mitochondrial tRNA aminoacylation is essential for the translation of the 13 mtDNA-encoded subunits of the oxidative phosphorylation system, and defects cause severe multisystem disorders [6,7].
• Mutations in mitochondrial aminoacyl-tRNA synthetases such as FARS2 cause cardiomyopathy by disrupting mitochondrial homeostasis and quality control.
• Aging-induced tRNA(Glu)-derived fragments can impair glutamate biosynthesis by targeting mitochondrial translation-dependent cristae organization, linking this process to metabolic aging.
• The editing activity of methionyl-tRNA synthetase, regulated by AIMP3, is critical for cardiac homeostasis, highlighting quality control in mitochondrial aminoacylation.
• CRISPR-based models (knockout, point mutation, knock-in, overexpression) enable causal dissection of genes involved in mitochondrial tRNA aminoacylation and their roles in disease [2,4].
Description
Mitochondria contain their own genome (mtDNA) that encodes 13 essential subunits of the oxidative phosphorylation (OXPHOS) complexes, along with the rRNAs and tRNAs required for their translation. The process of translating these mtDNA-encoded proteins depends on a dedicated set of mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs) that charge mitochondrial tRNAs with their cognate amino acids, a reaction defined by the Gene Ontology term GO:0070127: tRNA aminoacylation for mitochondrial protein translation [6,7]. This process occurs in the mitochondrial matrix and is essential for cellular energy production, and its dysfunction is increasingly linked to human disease [6,7]. Unlike cytoplasmic protein synthesis, mitochondrial translation uses a distinct set of tRNA synthetases, many of which are encoded by nuclear genes and imported into mitochondria. The aminoacylation reaction they catalyze is chemically identical to that in the cytoplasm but is spatially and genetically separate, making it a unique target for understanding mitochondrial biology and disease [6,7]. Defects in mitochondrial tRNA aminoacylation lead to impaired mitochondrial translation, respiratory chain deficiency, and a broad spectrum of clinical phenotypes including cardiomyopathy, encephalopathy, and metabolic disorders [2,6]. Recent studies have revealed additional layers of regulation, including editing activities of certain synthetases and the impact of tRNA-derived fragments on mitochondrial translation [1,8]. These findings underscore the importance of GO:0070127 not only for basic mitochondrial biology but also for therapeutic development. This article provides a comprehensive overview of the definition, mechanisms, key genes, disease associations, and research methods for studying tRNA aminoacylation for mitochondrial protein translation.
tRNA aminoacylation for mitochondrial protein translation At A Glance
| GO ID | GO:0070127 |
|---|---|
| GO term | tRNA aminoacylation for mitochondrial protein translation |
| Ontology | biological_process |
| Synonym | None |
| Definition | The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA, to be used in ribosome-mediated polypeptide synthesis in a mitochondrion. |
| Major function | Charging mitochondrial tRNAs with cognate amino acids for mitochondrial protein synthesis |
| Cellular location | Mitochondrial matrix |
| Key enzymes | Mitochondrial aminoacyl-tRNA synthetases (e.g., FARS2, AARS2, etc.) |
| Related process | Mitochondrial translation, oxidative phosphorylation |
What Is GO:0070127?
GO:0070127, tRNA aminoacylation for mitochondrial protein translation, is defined as the synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and an amino acid, to be used in ribosome-mediated polypeptide synthesis in a mitochondrion. In simpler terms, it is the process by which mitochondrial tRNAs are charged with their correct amino acids, preparing them for protein synthesis inside mitochondria.
Why Is tRNA aminoacylation for mitochondrial protein translation Important in Cell Biology?
Mitochondrial tRNA aminoacylation is indispensable for mitochondrial protein synthesis, which in turn is required for the assembly and function of the oxidative phosphorylation (OXPHOS) system, the primary source of cellular ATP. Defects in this process lead to a wide range of human disorders, often with severe clinical manifestations such as cardiomyopathy, encephalopathy, and lactic acidosis [2,6,7]. Understanding GO:0070127 is therefore critical for deciphering the molecular basis of mitochondrial diseases and for developing targeted therapies.
• Essential for the translation of 13 mtDNA-encoded OXPHOS subunits, which are core components of the electron transport chain.
• Mutations in mitochondrial aminoacyl-tRNA synthetases cause severe diseases including cardiomyopathy, encephalopathy, and developmental delay [2,6].
• Dysregulation of mitochondrial tRNA aminoacylation contributes to aging-related metabolic decline through tRNA-derived fragments.
• Quality control mechanisms, such as editing by methionyl-tRNA synthetase, are vital for cardiac homeostasis.
• Mitochondrial tRNA aminoacylation is a potential therapeutic target for mitochondrial diseases and metabolic disorders [2,7].
• The process is evolutionarily conserved and studied in model organisms like Arabidopsis, providing insights into tRNA aminoacylation landscapes.
• Aminoacyl-tRNA synthetase subunits can coordinate mitochondrial protein synthesis with mtDNA levels, linking translation to mitochondrial biogenesis.
• Threonyl-tRNA synthetase-like proteins exhibit both aminoacylation and editing activities, highlighting the complexity of mitochondrial tRNA charging.
• Defects in mitochondrial protein synthesis, including aminoacylation, are implicated in neurodegeneration and neuromuscular disorders [6,7].
What Happens During tRNA aminoacylation for mitochondrial protein translation?
Amino Acid Activation and tRNA Binding
In simple terms: The enzyme first attaches the amino acid to AMP, then transfers it to the tRNA.
Mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs) catalyze a two-step reaction: first, the amino acid is activated by ATP to form an aminoacyl-adenylate intermediate, releasing pyrophosphate; second, the aminoacyl group is transferred to the 3'-end of the cognate mitochondrial tRNA, forming an ester bond with the ribose of the terminal adenosine. This reaction is highly specific, ensured by the synthetase's recognition of tRNA identity elements. For example, FARS2 (phenylalanyl-tRNA synthetase 2, mitochondrial) charges tRNA(Phe) with phenylalanine, a step essential for mitochondrial translation.
Proofreading and Editing
In simple terms: Some enzymes double-check their work to prevent attaching the wrong amino acid.
Certain mitochondrial aminoacyl-tRNA synthetases possess editing activities that hydrolyze mischarged tRNAs, ensuring translational fidelity. For instance, a threonyl-tRNA synthetase-like protein has been shown to have both tRNA aminoacylation and editing activities. Similarly, the editing activity of methionyl-tRNA synthetase is regulated by AIMP3 and is critical for cardiac homeostasis. These quality control mechanisms prevent the incorporation of incorrect amino acids into mitochondrial proteins, which could otherwise lead to protein misfolding and mitochondrial dysfunction.
Delivery to the Mitochondrial Ribosome
In simple terms: The charged tRNA is then delivered to the ribosome to build proteins.
Once aminoacylated, the charged tRNA is bound by elongation factor Tu (EF-Tu) in the mitochondrial matrix and delivered to the mitochondrial ribosome (mitoribosome) for incorporation into the growing polypeptide chain. This step couples tRNA aminoacylation to mitochondrial protein synthesis. The mitoribosome translates the 13 mtDNA-encoded proteins, which are highly hydrophobic subunits of the OXPHOS complexes, and their proper synthesis depends on a steady supply of correctly charged tRNAs.
Coordination with mtDNA Levels and Mitochondrial Homeostasis
In simple terms: The charging process is linked to how much mitochondrial DNA is present and overall mitochondrial health.
Mitochondrial protein synthesis and mtDNA levels are coordinated through an aminoacyl-tRNA synthetase subunit, ensuring that translation capacity matches mitochondrial biogenesis demands. Disruption of this coordination, as seen in FARS2 deficiency, leads to impaired mitochondrial homeostasis and activation of the mitochondrial quality control system, contributing to cardiomyopathy. Thus, tRNA aminoacylation is not an isolated reaction but is integrated into the broader network of mitochondrial function and stress responses.
Impact of tRNA-Derived Fragments
In simple terms: Small pieces of tRNA can interfere with mitochondrial translation and metabolism.
Aging-induced tRNA(Glu)-derived fragments can impair glutamate biosynthesis by targeting mitochondrial translation-dependent cristae organization. These fragments likely interfere with the aminoacylation or delivery of tRNA(Glu), leading to reduced mitochondrial translation and altered cristae structure. This highlights a novel regulatory layer where tRNA fragments modulate GO:0070127 and downstream metabolic pathways, linking mitochondrial tRNA aminoacylation to aging and metabolic regulation.
Key Genes Involved in GO:0070127 tRNA aminoacylation for mitochondrial protein translation
The following genes encode key components of the mitochondrial tRNA aminoacylation machinery and related factors, with their roles and research relevance.
| Gene | Major Role | Research Relevance |
|---|---|---|
| FARS2 | Mitochondrial phenylalanyl-tRNA synthetase; charges tRNA(Phe) | Deficiency causes cardiomyopathy and mitochondrial homeostasis disruption |
| AARS2 | Mitochondrial alanyl-tRNA synthetase; charges tRNA(Ala) | Mutations linked to mitochondrial disorders and cardiomyopathy |
| MARS2 | Mitochondrial methionyl-tRNA synthetase; charges tRNA(Met) | Editing activity regulated by AIMP3; critical for cardiac homeostasis |
| TARS2 | Mitochondrial threonyl-tRNA synthetase; charges tRNA(Thr) | Mutations associated with mitochondrial encephalopathy |
| RARS2 | Mitochondrial arginyl-tRNA synthetase; charges tRNA(Arg) | Defects cause pontocerebellar hypoplasia |
| YARS2 | Mitochondrial tyrosyl-tRNA synthetase; charges tRNA(Tyr) | Mutations lead to myopathy, lactic acidosis, and sideroblastic anemia |
| SARS2 | Mitochondrial seryl-tRNA synthetase; charges tRNA(Ser) | Deficiency causes HUPRA syndrome |
| DARS2 | Mitochondrial aspartyl-tRNA synthetase; charges tRNA(Asp) | Mutations cause leukoencephalopathy with brainstem and spinal cord involvement |
| EARS2 | Mitochondrial glutamyl-tRNA synthetase; charges tRNA(Glu) | Deficiency leads to severe encephalopathy |
| AIMP3 | Regulates editing activity of methionyl-tRNA synthetase | Maintains cardiac homeostasis; potential therapeutic target |
| GARS | Glycyl-tRNA synthetase; also mitochondrial isoform | Mutations cause Charcot-Marie-Tooth disease |
| KARS | Lysyl-tRNA synthetase; mitochondrial and cytoplasmic | Mutations linked to neuropathy and cardiomyopathy |
| LARS2 | Mitochondrial leucyl-tRNA synthetase; charges tRNA(Leu) | Deficiency causes Perrault syndrome |
| PARS2 | Mitochondrial prolyl-tRNA synthetase; charges tRNA(Pro) | Mutations associated with developmental delay |
| NARS2 | Mitochondrial asparaginyl-tRNA synthetase; charges tRNA(Asn) | Defects cause Alpers syndrome and epilepsy |
| VARS2 | Mitochondrial valyl-tRNA synthetase; charges tRNA(Val) | Mutations linked to mitochondrial encephalopathy |
| IARS2 | Mitochondrial isoleucyl-tRNA synthetase; charges tRNA(Ile) | Deficiency causes cataract and growth retardation |
| CARS2 | Mitochondrial cysteinyl-tRNA synthetase; charges tRNA(Cys) | Mutations associated with progressive myoclonic epilepsy |
How Is tRNA aminoacylation for mitochondrial protein translation Regulated?
The process of mitochondrial tRNA aminoacylation is regulated at multiple levels. The expression of nuclear-encoded mitochondrial aminoacyl-tRNA synthetases is coordinated with mitochondrial biogenesis through signaling pathways such as PGC-1alpha and mTOR, although direct evidence in the context of GO:0070127 is still emerging. Additionally, the editing activity of certain synthetases, such as methionyl-tRNA synthetase, is modulated by interacting proteins like AIMP3, which ensures translational fidelity and cardiac homeostasis. Furthermore, aminoacyl-tRNA synthetase subunits can sense mtDNA levels and adjust mitochondrial protein synthesis accordingly, providing a feedback mechanism to maintain mitochondrial proteostasis. Aging-induced tRNA-derived fragments can also inhibit mitochondrial translation, representing a post-transcriptional regulatory layer.
tRNA aminoacylation for mitochondrial protein translation and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| FARS2 | Cardiomyopathy, mitochondrial homeostasis disruption | Knockout mouse, patient-derived iPSC-cardiomyocytes |
| MARS2 | Cardiac homeostasis, editing activity dysregulation | Knock-in mouse with editing-deficient MARS2, AIMP3 knockout |
| DARS2 | Leukoencephalopathy with brainstem and spinal cord involvement | Knockout mouse, patient fibroblasts |
| YARS2 | Myopathy, lactic acidosis, sideroblastic anemia | Knockout zebrafish, patient iPSC-derived muscle cells |
| EARS2 | Severe encephalopathy | Knockout mouse, patient-derived neurons |
Mitochondrial Cardiomyopathy
Mutations in genes encoding mitochondrial aminoacyl-tRNA synthetases, such as FARS2, cause severe cardiomyopathy by disrupting mitochondrial homeostasis and the mitochondrial quality control system. FARS2 deficiency leads to impaired mitochondrial translation, reduced OXPHOS complex assembly, and activation of the mitochondrial unfolded protein response, ultimately resulting in cardiac dysfunction. This highlights the critical role of GO:0070127 in heart function and disease.
Neurodegenerative and Neuromuscular Disorders
Defects in mitochondrial tRNA aminoacylation are associated with a spectrum of neurological disorders, including encephalopathy, epilepsy, and peripheral neuropathy [6,7]. For example, mutations in DARS2 cause leukoencephalopathy with brainstem and spinal cord involvement, while YARS2 mutations lead to myopathy and sideroblastic anemia. These conditions underscore the vulnerability of high-energy-demand tissues like the brain and muscle to impaired mitochondrial translation.
Metabolic and Aging-Related Disorders
Aging-induced tRNA(Glu)-derived fragments impair glutamate biosynthesis by targeting mitochondrial translation-dependent cristae organization, linking GO:0070127 to metabolic aging. This mechanism may contribute to age-related metabolic decline and neurodegeneration. Additionally, the editing activity of methionyl-tRNA synthetase, regulated by AIMP3, is essential for cardiac homeostasis, and its dysregulation may contribute to age-related cardiac dysfunction.
From tRNA aminoacylation for mitochondrial protein translation-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of FARS2 cause cardiomyopathy? | FARS2 knockout mouse and iPSC-derived cardiomyocytes |
| What is the role of MARS2 editing activity in cardiac homeostasis? | MARS2 point-mutation knock-in mouse (editing-deficient) |
| How does AIMP3 regulate methionyl-tRNA synthetase? | AIMP3 knockout mouse and overexpression cell lines |
| Does a specific tRNA synthetase mutation affect mitochondrial translation? | Knock-in mouse carrying patient mutation, cellular respiration assays |
| Can overexpression of a synthetase rescue mitochondrial defects? | Overexpression of wild-type or mutant synthetase in patient fibroblasts |
| What is the impact of tRNA-derived fragments on mitochondrial translation? | Inducible overexpression of tRNA fragments in cell lines |
How to Study the tRNA aminoacylation for mitochondrial protein translation Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Ribo-seq | Mitochondrial translation efficiency and ribosome occupancy | Assessing impact of synthetase mutations on mitochondrial protein synthesis |
| tRNA-seq | tRNA abundance and charging levels | Detecting uncharged tRNA accumulation in disease models |
| Small RNA-seq | tRNA-derived fragments | Identifying regulatory tRNA fragments in aging and disease |
| Proteomics | Mitochondrial protein levels and OXPHOS assembly | Quantifying translation products and complex assembly |
| Western blot | Specific mitochondrial protein expression | Validating changes in mtDNA-encoded proteins |
| Blue-native PAGE | OXPHOS complex assembly | Assessing respiratory chain supercomplexes |
| Seahorse assay | Oxygen consumption rate and glycolysis | Measuring mitochondrial respiratory function |
| Fluorescence microscopy | Mitochondrial morphology and cristae structure | Visualizing mitochondrial network and cristae organization |
Ribosome Profiling (Ribo-seq)
Ribo-seq can be adapted to measure mitochondrial translation by isolating mitochondrial ribosomes and sequencing protected mRNA fragments. This method reveals the efficiency of mitochondrial protein synthesis and the impact of defective tRNA aminoacylation on ribosome pausing and codon occupancy. It is particularly useful for studying how mutations in aminoacyl-tRNA synthetases affect translation elongation in mitochondria.
RNA Sequencing and tRNA Quantification
RNA-seq and specialized tRNA-seq methods can quantify mitochondrial tRNA levels and charging status. These approaches help assess whether defects in aminoacylation lead to accumulation of uncharged tRNAs, which can trigger stress responses. Additionally, small RNA sequencing can detect tRNA-derived fragments that may regulate mitochondrial translation.
Proteomics and Western Blotting
Proteomic analysis of mitochondrial fractions can reveal changes in OXPHOS subunit levels and assembly. Western blotting for specific mitochondrial proteins, such as those encoded by mtDNA, assesses the functional consequences of impaired tRNA aminoacylation. Blue-native PAGE can further evaluate the assembly of oxidative phosphorylation complexes.
Imaging and Functional Assays
Fluorescence microscopy with mitochondrial markers (e.g., MitoTracker) and cristae-staining dyes can visualize mitochondrial morphology and cristae organization, which are affected by defective mitochondrial translation. Seahorse extracellular flux analysis measures oxygen consumption rates to assess mitochondrial respiratory function in cells with manipulated aminoacylation genes.
How CRISPR Can Be Used to Study GO:0070127 tRNA aminoacylation for mitochondrial protein translation
Knockout
CRISPR-Cas9 knockout of mitochondrial aminoacyl-tRNA synthetase genes (e.g., FARS2, MARS2) in cell lines or animal models can recapitulate disease phenotypes such as impaired mitochondrial translation and respiratory chain deficiency. Knockout models are essential for determining the loss-of-function consequences and for testing rescue strategies.
Point Mutation
Introducing patient-specific point mutations (e.g., in FARS2 or MARS2) using CRISPR base editing or homology-directed repair allows precise modeling of disease-associated variants [2,8]. These models help distinguish between loss-of-function and gain-of-function effects and assess the impact on tRNA aminoacylation and editing activities.
Knock-in
Knock-in of tagged versions of aminoacyl-tRNA synthetases (e.g., HA-tagged FARS2) enables localization, interaction, and functional studies. Knock-in of reporter genes under the control of endogenous promoters can also monitor expression dynamics in response to mitochondrial stress.
Overexpression
CRISPR activation (CRISPRa) or lentiviral overexpression of wild-type or mutant aminoacyl-tRNA synthetases can rescue or exacerbate mitochondrial defects. Overexpression studies are useful for structure-function analysis and for identifying dominant-negative effects [4,8].
How EDITGENE Supports tRNA aminoacylation for mitochondrial protein translation Research
Researchers studying tRNA aminoacylation for mitochondrial protein translation-related genes often need to determine whether a candidate gene is causally involved in mitochondrial dysfunction and disease. This requires precise genetic models that can mimic human mutations, knock out gene function, or overexpress specific variants. EDITGENE provides a comprehensive suite of CRISPR-based services to accelerate such investigations, from knockout cell lines to knock-in mice and library screening.
Contact EDITGENE today to design your custom CRISPR model for tRNA aminoacylation for mitochondrial protein translation research.
Frequently Asked Questions About tRNA aminoacylation for mitochondrial protein translation
What is GO:0070127?
GO:0070127 is the Gene Ontology term for tRNA aminoacylation for mitochondrial protein translation, the process of charging mitochondrial tRNAs with amino acids for protein synthesis inside mitochondria.
What genes are involved in tRNA aminoacylation for mitochondrial protein translation?
Key genes include mitochondrial aminoacyl-tRNA synthetases such as FARS2, AARS2, MARS2, TARS2, RARS2, YARS2, SARS2, DARS2, EARS2, and others, each charging a specific tRNA [6,7].
Why is mitochondrial tRNA aminoacylation important?
It is essential for synthesizing the 13 mtDNA-encoded subunits of the oxidative phosphorylation system, which produces most cellular ATP. Defects cause severe mitochondrial diseases.
What diseases are linked to defects in mitochondrial tRNA aminoacylation?
Diseases include cardiomyopathy, encephalopathy, leukoencephalopathy, myopathy, sideroblastic anemia, and metabolic disorders, depending on the affected gene [2,6,7].
How can CRISPR be used to study mitochondrial tRNA aminoacylation?
CRISPR knockout, point mutation, knock-in, and overexpression models allow researchers to mimic human mutations, assess loss- or gain-of-function, and test rescue strategies in cells and animals [2,4,8].
What is the role of FARS2 in mitochondrial translation?
FARS2 encodes mitochondrial phenylalanyl-tRNA synthetase, which charges tRNA(Phe). Its deficiency causes cardiomyopathy by disrupting mitochondrial homeostasis and quality control.
How is mitochondrial tRNA aminoacylation regulated?
It is regulated by expression of synthetases, editing activities (e.g., MARS2 regulated by AIMP3), coordination with mtDNA levels, and tRNA-derived fragments [1,4,8].
What methods are used to study mitochondrial tRNA aminoacylation?
Methods include Ribo-seq, tRNA-seq, proteomics, Western blot, blue-native PAGE, Seahorse assays, and fluorescence microscopy [1,2,3,6].
Can tRNA-derived fragments affect mitochondrial translation?
Yes, aging-induced tRNA(Glu)-derived fragments impair glutamate biosynthesis by targeting mitochondrial translation-dependent cristae organization.
What model systems are available for studying mitochondrial tRNA aminoacylation?
Models include knockout mice, patient-derived iPSCs, knock-in mice with point mutations, overexpression cell lines, and CRISPR screens [2,4,8].
Conclusion
GO:0070127, tRNA aminoacylation for mitochondrial protein translation, is a fundamental biological process required for mitochondrial energy production and cellular homeostasis. Defects in this pathway lead to a wide range of human diseases, particularly those affecting high-energy tissues such as heart and brain. Recent research has uncovered intricate regulatory mechanisms, including editing activities and tRNA-derived fragments, that fine-tune mitochondrial translation. Leveraging CRISPR-based models and advanced omics technologies will be crucial for dissecting the molecular mechanisms and developing therapeutic interventions for mitochondrial diseases.
References
- 1. Li D et al.. 2024. Aging-induced tRNA(Glu)-derived fragment impairs glutamate biosynthesis by targeting mitochondrial translation-dependent cristae organization.. Cell Metab 36(5):1059-1075.e9 PMID: 38458203
- 2. Li B et al.. 2024. FARS2 Deficiency Causes Cardiomyopathy by Disrupting Mitochondrial Homeostasis and the Mitochondrial Quality Control System.. Circulation 149(16):1268-1284 PMID: 38362779
- 3. Ceriotti LF et al.. 2024. The landscape of Arabidopsis tRNA aminoacylation.. Plant J 120(6):2784-2802 PMID: 39555621
- 4. Picchioni D et al.. 2019. Mitochondrial Protein Synthesis and mtDNA Levels Coordinated through an Aminoacyl-tRNA Synthetase Subunit.. Cell Rep 27(1):40-47.e5 PMID: 30943413
- 5. Chen Y et al.. 2018. A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities.. Nucleic Acids Res 46(7):3643-3656 PMID: 29579307
- 6. Jacobs HT. 2003. Disorders of mitochondrial protein synthesis.. Hum Mol Genet 12 Spec No 2:R293-301 PMID: 12928485
- 7. Abbott JA et al.. 2014. Transfer RNA and human disease.. Front Genet 5:158 PMID: 24917879
- 8. Das AS et al.. 2025. AIMP3 maintains cardiac homeostasis by regulating the editing activity of methionyl-tRNA synthetase.. Nat Cardiovasc Res 4(7):876-890 PMID: 40562875
