bims-mirnam Biomed News
on Mitochondrial RNA metabolism
Issue of 2026–01–11
sixteen papers selected by
Hana Antonicka, McGill University



  1. Mol Cell. 2026 Jan 08. pii: S1097-2765(25)01013-5. [Epub ahead of print]86(1): 6-8
      In this issue of Molecular Cell, Zhu et al.1 show that mitochondria of cancer cells rely on the import of glutamine not only to fuel metabolite synthesis via the tricarboxylic acid cycle but also to charge mt-tRNAGln to allow mitochondrial protein synthesis and respiration.
    DOI:  https://doi.org/10.1016/j.molcel.2025.12.014
  2. bioRxiv. 2025 Dec 30. pii: 2025.12.30.697032. [Epub ahead of print]
      Translation initiation, the first step of the translation cycle, involves initiation factors (mtIF) 2 and 3 in mitochondria. mtIF3 release from the ribosomal small subunit was believed to be a prerequisite for the recruitment of the initiator tRNA. Here we use cryogenic electron microscopy to characterize plant mitochondria pre-initiation complexes and to reveal how plant mtIF3 binds the initiator tRNA and facilitates its accommodation in the decoding center.
    DOI:  https://doi.org/10.64898/2025.12.30.697032
  3. bioRxiv. 2025 Dec 23. pii: 2025.12.21.693523. [Epub ahead of print]
      Outer mitochondrial membranes (OMM) function as dynamic hubs for inter-organelle communication, integrating bidirectional signals, and coordinating organelle behavior in a context-dependent manner. However, tools for mapping mitochondrial surface proteomes with high spatial and temporal resolution remain limited. Here, we introduce an optogenetic proximity labeling strategy using LOV-Turbo, a light-activated biotin ligase, to profile mitochondrial surface proteomes with improved precision, temporal control, and reduced background. By fusing LOV-Turbo to a panel of variants of an OMM-anchored protein, Miro1, we generate spatially distinct baits that resolve modular architectures and regulatory states of the OMM proteomes across diverse conditions, a database we name MitoSurf. Building on this proteomic map, we present RiboLOOM, a platform that defines LOV-Turbo labeled ribosomes and their bound mRNAs at the mitochondrial surface. MitoSurf and RiboLOOM uncover a spatially distinct ribosome pool at the OMM that is maintained by Miro1, enabling local mRNA engagement and translation of mitochondria-related proteins. These findings establish Miro1 as a key organizer of mitochondrial protein biogenesis through spatial confinement of surface-associated ribosomes. Our platform reveals an uncharted layer of mitochondrial surface biology and provides a generalizable strategy to dissect dynamic RNA-protein-organelle interfaces in living cells.
    DOI:  https://doi.org/10.64898/2025.12.21.693523
  4. MedComm (2020). 2026 Jan;7(1): e70572
      Ischemic heart disease is one of the diseases with the highest morbidity and mortality in the world. The N7-methylguanosine (m7G) tRNA modifications are widely recognized as one of the most prevalent tRNA modifications. Nevertheless, there is still a lack of understanding regarding the roles and molecular mechanisms underlying the METTL1-mediated m7G tRNA modification in cardiac ischemia/reperfusion (I/R) injury. METTL1 and m7G tRNA modification were upregulated in mice with I/R injury hearts and the plasma of patients with acute myocardial infarction. Thus, we constructed METTL1 knockout mice and found that silencing METTL1 alleviates I/R. Mechanistically, tRNA sequencing, MeRIP-m7G-tRNA sequencing, and Ribosome profiling sequencing were used to clarify deficiency of METTL1 reduced the levels of m7G tRNA modifications and m7G-modified tRNAs, and consequently, downregulated the translation efficiency of ATPIF1 mRNA to restore the level of mitochondrial oxidative phosphorylation and suppress the increase of mitochondrial apoptosis. Moreover, cardiac-specific overexpression of ATPIF1 induced myocardial hypertrophy and inhibited the protective effect of silencing METTL1 on cardiac I/R injury. Collectively, m7G tRNA modifications regulate the translation efficiency of ATPIF1, which eventually mediates mitochondrial energy metabolism, apoptosis, and myocardial I/R injury. The findings uncover that interfering with METTL1 and ATPIF1 represents a novel therapeutic target in myocardial I/R injury.
    Keywords:  METTL1; m7G tRNA modification; mitochondrial energy metabolism; myocardial ischemia/reperfusion injury
    DOI:  https://doi.org/10.1002/mco2.70572
  5. J Inherit Metab Dis. 2026 Jan;49(1): e70139
      MRPS genes, which encode components of the small mitoribosomal subunit, have not been previously linked to adult-onset neurological diseases. These genes play a critical role in mitochondrial translation and the biogenesis of the oxidative phosphorylation system. Whole Genome Sequencing was performed on adult patients presenting with an unexplained neurological picture. In parallel, functional studies were carried out in patient-derived fibroblasts to assess mitochondrial translation and the status of oxidative phosphorylation pathways. Bi-allelic pathogenic variants in MRPS22, MRPS23, and MRPS34 were identified in four patients from unrelated families. All patients presented a similar complex neurological phenotype, including cerebellar ataxia, distal motor neuropathy, pyramidal syndrome, and a distinctive leukoencephalopathy on brain MRI. Additional findings included elevated cerebrospinal fluid (CSF) protein levels and profound cerebral folate deficiency. Functional analyses revealed impaired mitochondrial translation and multiple defects in oxidative phosphorylation. Treatment with oral folinic acid resulted in clinical stabilization, radiological improvement, and normalization of CSF 5-methyltetrahydrofolate levels. Our findings expand the spectrum of mitochondrial diseases caused by defects in mitoribosomal proteins, highlighting their role in adult-onset neurological disorders with distinctive brain imaging features, high CSF protein levels, and cerebral folate deficiency.
    Keywords:  cerebral folate deficiency; distal motor neuropathy; leukoencephalopathy; mitoribosome
    DOI:  https://doi.org/10.1002/jimd.70139
  6. J Cell Biol. 2026 Apr 06. pii: e202507116. [Epub ahead of print]225(4):
      Hundreds of mitochondrial proteins rely on N-terminal presequences for organellar targeting and import. While generally described as positively charged amphiphilic helices, presequences lack a consensus motif and thus likely promote protein import into mitochondria with variable efficiencies. Indeed, the concept of presequence strength underlies biological models such as stress sensing, yet a quantitative analysis of what dictates strong versus weak presequences is lacking. Furthermore, the extent to which presequence strength affects mitochondrial function and cellular fitness remains unclear. Here, we capitalize on the MitoLuc protein import assay to define multiple aspects of presequence strength. We find that select presequences, including those that regulate the mitochondrial unfolded protein response (UPRmt), impart differential import efficiencies during mitochondrial uncoupling. Surprisingly, we find that presequences beyond those associated with stress signaling promote highly variable import efficiency in vitro, suggesting presequence strength may influence a broader array of processes than currently appreciated. We exploit this variability to demonstrate that only presequences that promote robust in vitro import can fully rescue defects in respiratory growth in complex IV-deficient yeast, suggesting that presequence strength dictates metabolic potential. Collectively, our findings demonstrate that presequence strength can describe numerous metrics, such as total imported protein, maximal import velocity, or sensitivity to uncoupling, suggesting that the annotation of presequences as weak or strong requires more nuanced characterization than typically performed. Importantly, we find that such variability in presequence strength meaningfully affects cellular fitness beyond stress signaling, suggesting that organisms may broadly exploit presequence strength to fine-tune mitochondrial import and thus organellar homeostasis.
    DOI:  https://doi.org/10.1083/jcb.202507116
  7. Curr Opin Plant Biol. 2026 Jan 07. pii: S1369-5266(25)00165-7. [Epub ahead of print]89 102851
      Modified nucleotides on RNAs have been investigated for over six decades for their potential role in regulating gene expression and protein synthesis across a wide range of organisms, from animals to plants and fungi, as well as in viral genetic materials. Among them, mRNA methylation stands out with its dynamic nature, which underscores the adaptability of the epitranscriptome in developmental transitions and response to environmental stress, especially in plants. Advances in next-generation sequencing methods have revealed the specific sequence contexts of mRNA methylation, uncovering their involvement in gene regulatory networks. Additionally, genetic perturbations on the writers, erasers, and readers of m6A and m5C expanded our understanding of the physiological function and the mode of action of these modifications. In this review, we highlight recent advances in understanding how mRNA fate decisions, mainly determined by m6A and m5C RNA methylation, shape stress response and development in plants.
    DOI:  https://doi.org/10.1016/j.pbi.2025.102851
  8. bioRxiv. 2025 Dec 22. pii: 2025.12.19.694874. [Epub ahead of print]
      The spatiotemporal organization of multiple components within biomolecular condensates helps coordinate gene expression. Mitochondria separate transcription and RNA processing into two distinct condensates: mt-nucleoids and mtRNA granules (MRGs), respectively. However, how mtRNA transcripts are transferred from mt-nucleoids to distant MRGs was unclear. With high-resolution imaging, we examined the steady-state organization of mt-condensates in human cells. We identified a wide distribution of distances between centroids of mt-condensates, from roughly a micron apart to within 100 nm of each other. Live imaging revealed that such organization was dynamic: mt-condensates frequently underwent cycles of mixing and demixing. Indeed, mtRNA transcripts and the mtRNA polymerase co-localized within mixed mt-condensates, while transcription inhibition led to complete dissolution of MRGs, supporting that nascently transcribed mtRNA is a key driver of mt-condensate organization. Together, our results show that active transcription sustains the phase coexistence between mt-nucleoids and MRGs, with implications for transcriptional condensates more broadly.
    DOI:  https://doi.org/10.64898/2025.12.19.694874
  9. Ann Med Surg (Lond). 2026 Jan;88(1): 1019-1020
      Kearns-Sayre syndrome (KSS) is a rare mitochondrial disorder defined by a combination of ophthalmoplegia, pigmentary retinopathy, and cardiac conduction defects. KSS arises from mitochondrial DNA (mtDNA) deletions and heteroplasmic imbalance, where there is a variation in levels of normal versus abnormal mtDNA. Current therapies offer symptomatic relief at most; they do not address the primary issue of correcting the genetic mutation. Innovative methods employing CRISPR Prime Editing (PE), an accurate and RNA-less technology, allow for unique correction of pathogenic mtDNA variants and errors. By fixing the wild type to variant ratio, PE could directly correct ocular- and cardiac-related signs and symptoms in KSS, in two tissue types that are entirely dependent on mitochondrial bioenergetics for their energy needs. Furthermore, the use of tissue-specific delivery methods, such as AAV2 vectors or cardiomyocyte promoters, would further enhance the targeting of the corrective approach to more specifically correct disease processes. This represents a completely innovative approach to genomic correction in the field of mitochondrial medicine, and there is important to translate this research to the clinic.
    DOI:  https://doi.org/10.1097/MS9.0000000000004366
  10. PLoS Genet. 2026 Jan 09. 22(1): e1011836
      The mitochondrial genome (mtDNA) encodes essential subunits of the electron transport chain and ATP synthase. Mutations in these genes impair oxidative phosphorylation, compromise mitochondrial ATP production and cellular energy supply, and can cause mitochondrial diseases. These consequences highlight the importance of mtDNA quality control (mtDNA-QC), the process by which cells selectively maintain intact mtDNA to preserve respiratory function. Here, we developed a high-throughput flow cytometry assay for Saccharomyces cerevisiae to track mtDNA segregation in cell populations derived from heteroplasmic zygotes, in which wild-type (WT) mtDNA is fluorescently labeled and mutant mtDNA remains unlabeled. Using this approach, we observe purifying selection against mtDNA lacking subunits of complex III (COB), complex IV (COX2) or the ATP synthase (ATP6), under fermentative conditions that do not require respiratory activity. By integrating cytometric data with growth assays, qPCR-based mtDNA copy-number measurements, and simulations, we find that the decline of mtDNAΔatp6 in populations derived from heteroplasmic zygotes is largely explained by the combination of its reduced mtDNA copy number-biasing zygotes toward higher contributions of intact mtDNA-and the proliferative disadvantage of cells carrying this variant. In contrast, the loss of mtDNAΔcob and mtDNAΔcox2 cannot be explained by growth defects and copy-number asymmetries alone, indicating an additional intracellular selection against these mutant genomes when intact mtDNA is present. In heteroplasmic cells containing both intact and mutant mtDNA, fluorescent reporters revealed local reductions in ATP levels and membrane potential ([Formula: see text]) near mutant genomes, indicating spatial heterogeneity in mitochondrial physiology that reflects local mtDNA quality. Disruption of the respiratory chain by deletion of nuclear-encoded subunits (RIP1, COX4) abolished these physiological gradients and impaired mtDNA-QC, suggesting that local bioenergetic differences are required for selective recognition. Together, our findings support a model in which yeast cells assess local respiratory function as a proxy for mtDNA integrity, enabling intracellular selection for functional mitochondrial genomes.
    DOI:  https://doi.org/10.1371/journal.pgen.1011836
  11. Commun Biol. 2026 Jan 08.
      Mitochondria respond to various stresses. Nevertheless, the regulation of this response while considering coordination between mitochondrial (mtDNA)- and nuclear DNA (nDNA)-encoded gene expression has been overlooked. Our RNA-seq analysis of 18 human cell lines grown in hypoxia (0.2-2% oxygen, 16-24 h) reveals a significant and coordinated reduction of mito-nuclear oxidative phosphorylation (OXPHOS) genes' expression in most (N = 11) cell lines. mtDNA copy number assessment in U87, HCT-116, MCF-7, and HeLa cells reveals non-significant changes, suggesting that the overall reduced mito-nuclear gene expression (MNGE) in hypoxia occurs at the RNA level. Analysis of HIF1α ChIP-seq experiments from cells exposed to hypoxia reveals increased binding to upstream regulatory elements of certain regulators of mitochondrial gene expression. Furthermore, RNA-seq analysis of HIF1α knockout HCT-116 cells grown in hypoxia reveals reduced mtDNA gene expression, yet no change in nDNA OXPHOS genes, suggesting that HIF1α knockout led to departure from coordination of MNGE. Finally, nascent RNA transcripts analysis (PRO-seq) in HeLa, U87, and D407 cells grown in hypoxia shows increased intensity of pausing sites throughout the mtDNA. This finding suggests an important role for transcriptional pausing in the regulation of mtDNA gene expression. Taken together, coordinated reduction of MNGE in hypoxia underlines MNGE as a pivotal player in general mitochondrial function, and particularly in response to stress.
    DOI:  https://doi.org/10.1038/s42003-025-09457-y
  12. bioRxiv. 2025 Dec 26. pii: 2025.12.23.696290. [Epub ahead of print]
      Though ribosomes have several features that help them maintain their reading frame, these safeguards can be bypassed by RNA structures that promote -1 programmed ribosomal frameshifting (-1PRF). We recently found that conformational transitions in the nascent polypeptide can enhance -1PRF, though it's unclear whether this feedback plays a general role in translational recoding. Here we demonstrate that the translocation of nascent transmembrane domains is sufficient to induce -1PRF during the decoding of slippery heptamers. We identify thousands of motifs that potentially trigger -1PRF along with proteomic identifications of 33 predicted human frameshift products. We also identify thousands of splicing-dependent motifs and demonstrate that the splicing-mediated reconfiguration of transmembrane domains alters -1PRF. Finally, we show that most transcripts bearing these motifs are sensitive to the nonsense-mediated decay regulator UPF1, suggesting they modulate mRNA turnover. Our findings show that the misassembly of growing polypeptides can trigger -1PRF, premature termination, and transcript decay.
    DOI:  https://doi.org/10.64898/2025.12.23.696290
  13. Expert Opin Ther Targets. 2026 Jan 05.
       INTRODUCTION: Oxidative phosphorylation (OXPHOS) is essential for the progression of tumors and their resistance to therapy. Conventional inhibitors of OXPHOS that directly targeting the electron transport chain (ETC) activity often lack tumor selectivity and demonstrate limited efficacy. Inhibiting mitochondrial gene expression to block the de novo biogenesis of OXPHOS complexes - rather than inhibiting preexisting OXPHOS complexes - represents a more potent and tumor-selective strategy. This strategy highlights leucine-rich pentatricopeptide repeat-containing (LRPPRC) as a promising anticancer target.
    AREAS COVERED: Extensive evidence confirms that LRPPRC is commonly overexpressed in various cancer types and is indispensable for maintaining malignant phenotypes. Mechanistically, LRPPRC binds mitochondrial mRNAs (mt-mRNAs) via its pentatricopeptide repeat (PPR) motif-rich RNA-binding domain. By stabilizing mt-mRNA and enhancing its translational efficiency, LRPPRC facilitates OXPHOS complex biogenesis and OXPHOS in tumors. We have developed the first small molecule screening platform targeting LRPPRC. Using this platform, we identified dual-function compounds that both inhibit LRPPRC's RNA-binding function and trigger its proteolytic degradation. These agents demonstrate potent suppression of OXPHOS and exhibit favorable safety profiles across multiple preclinical models.
    EXPERT OPINION: Current LRPPRC inhibitors often suffer from suboptimal specificity and binding affinity. Advancing clinical translation requires co-crystal structures of LRPPRC for rational drug design and novel delivery strategies to enhance mitochondrial enrichment of inhibitors.
    Keywords:  LRPPRC; OXPHOS; RNA binding protein; small molecular inhibitors; targeted therapy
    DOI:  https://doi.org/10.1080/14728222.2025.2608028
  14. Cell Death Dis. 2026 Jan 07. 17(1): 4
      Cancer has become a leading cause of mortality worldwide, with alarming increases in incidence and mortality rates. Emerging evidence suggests that tRNA modification enzymes play a crucial role in cancer development by modulating codon-specific translation. In this review, we focus on 18 tRNA modification enzymes and elucidate their mechanisms of action and roles in disease. We highlight the functions and mechanisms of seven tRNA regulators that mediate favorable tRNA translation in tumorigenesis and cancer progression, providing deeper insights into their clinical potential as cancer-related biomarkers and prognostic indicators. These findings emphasize the need for further investigation into the therapeutic potential of tRNA modification enzymes in cancer management and their potential application in personalized cancer therapy and diagnostics.
    DOI:  https://doi.org/10.1038/s41419-025-08234-3
  15. Cell Death Discov. 2026 Jan 08.
      In the present study, we aimed to investigate the antioxidant and therapeutic protective effects of carvacryl acetate (CAA) on Mitochondrial damage of cerebral ischemia-reperfusion through mitochondrial transcription factor A (TFAM) signaling molecules.SD rats were used to establish the middle cerebral artery occlusion (MCAO) model in vivo, and PC12 cells were stimulated with H2O2 in vitro. Longa neurological score and triphenyltetrazolium chloride (TTC) staining was used to observe the ischemic infarction. Transmission electron microscope (TEM) was used to observe the mitochondria. Reactive Oxygen Species/ Superoxide Dismuptase/Malondialdehyde/Adenosine Triphosphate (ROS/SOD/MDA/ATP) detection kit was used to detect. RT-qPCR was used to detect the mRNA level of target gene and mitochondrial DNA (mtDNA) copy number changes. Immunofluorescence and Western blot were used to detect the expression of protein. After oxidative stress in the MCAO model of SD rats, the neurological score increased, the volume of ischemic area of cerebral infarction increased, the morphology of nerve cells in brain tissue and PC12 cells was disordered, the mitochondria appeared vacuolated, the contents of ROS and MDA increased, and the activity of SOD decreased. Oxidative stress causes mitochondrial dysfunction, resulting in the reduction of mtDNA copy number and the decreased expression of TFAM in brain tissue nerve cells and PC12 cells, which in turn affects mitochondrial transcription biogenesis and decreases the expression of POLRMT and TFB2M molecules. CAA promotes intracellular TFAM expression and activates its antioxidant pathway, thereby protecting mtDNA and alleviating oxidative stress and mitochondrial damage caused by MCAO in vivo and H2O2 stimulation in vitro. Lentivirus downregulates the expression of TFAM, and under its action, the antioxidant and mitochondrial protection effects of CAA are weakened. When TFAM was disrupted, the protective effect of CAA on mitochondria was inhibited. Compared to edaravone, a positive control, CAA exhibited similar therapeutic effects. These findings suggest that CAA alleviates CIRI through TFAM signaling pathways, offering potential therapeutic implications for ischemic stroke treatment.
    DOI:  https://doi.org/10.1038/s41420-025-02930-x
  16. bioRxiv. 2025 Dec 23. pii: 2025.12.19.695597. [Epub ahead of print]
      Metabolic enzymes can influence chromatin organization by modulating the availability of key metabolites, yet how specific metabolic reactions affect chromatin function remains poorly understood. Here, we show that in Caenorhabditis elegans, the methionine-cycle enzyme methionine synthase reductase (MTRR-1/MSR) regulates heterochromatin independently of methionine synthesis. Loss of MTRR-1, but not of the methionine synthase METR-1/MS, specifically reduces heterochromatic histone methylation, derepresses repetitive elements, and causes developmental delay. Multi-omics profiling revealed that mtrr-1 mutants activate transcriptional programs associated with mitochondrial stress and accumulate long-chain acylcarnitines, indicating disrupted mitochondrial homeostasis. Functional assays confirmed altered mitochondrial respiration in mtrr-1 mutants, while direct perturbation of mitochondrial function was sufficient to induce heterochromatin defects. Together, our results reveal a previously unrecognized mitochondria-to-chromatin axis controlled by the methionine-cycle enzyme MTRR-1/MSR.
    DOI:  https://doi.org/10.64898/2025.12.19.695597