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Cited by 14RNA and protein synthesis mechanismsRNA modifications and cancerMitochondrial Function and Pathology

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The mitochondrial methylation potential gates mitoribosome assembly

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Glasgow, Ruth I. C., Singh, Vivek, Peña-Pérez, Lucía, Wilhalm, Alissa, Moedas, Marco F., Moore, David, Rosenberger, Florian A., Li, Xinping, Atanassov, Ilian, Saba, Mira, Cipullo, Miriam, Rorbach, Joanna, Wedell, Anna, Freyer, Christoph, Amunts, Alexey, Wredenberg, Anna·2025·Nature Communications
DOI 10.1038/s41467-025-60977-xPMC PMC12198368

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Abstract

S-adenosylmethionine (SAM) is the principal methyl donor in cells and is essential for mitochondrial gene expression, influencing RNA modifications, translation, and ribosome biogenesis. Using direct long-read RNA sequencing in mouse tissues and embryonic fibroblasts, we show that processing of the mitochondrial ribosomal gene cluster fails in the absence of mitochondrial SAM, leading to an accumulation of unprocessed precursors. Proteomic analysis of ribosome fractions revealed these precursors associated with processing and assembly factors, indicating stalled biogenesis. Structural analysis by cryo-electron microscopy demonstrated that SAM-dependent methylation is required for peptidyl transferase centre formation during mitoribosome assembly. Our findings identify a critical role for SAM in coordinating mitoribosomal RNA processing and large subunit maturation, linking cellular methylation potential to mitochondrial translation capacity.

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  1. Monné, M., Marobbio, C. M. T., Agrimi, G., Palmieri, L. & Palmieri, F. Mitochondrial transport and metabolism of the major methyl donor and versatile cofactor S‐adenosylmethionine, and related diseases: a review†. IUBMB Life 74, 573–591 (2022). · DOI
  2. Suzuki, T. et al. Complete chemical structures of human mitochondrial tRNAs. Nat. Commun. 11, 4269 (2020). · DOI
  3. Sanchez, M. I. G. L., Cipullo, M., Gopalakrishna, S., Khawaja, A. & Rorbach, J. Methylation of ribosomal RNA: a mitochondrial perspective. Front. Genet. 11, 761 (2020). · DOI
  4. Rosenberger, F. A. et al. The one-carbon pool controls mitochondrial energy metabolism via complex I and iron-sulfur clusters. Sci. Adv. 7, eabf0717 (2021). · DOI
  5. Ojala, D., Montoya, J. & Attardi, G. tRNA punctuation model of RNA processing in human mitochondria. Nature 290, 470–474 (1981). · DOI
  6. Holzmann, J. et al. RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell 135, 462–474 (2008). · DOI
  7. Brzezniak, L. K., Bijata, M., Szczesny, R. J. & Stepien, P. P. Involvement of human ELAC2 gene product in 3’ end processing of mitochondrial tRNAs. RNA Biol. 8, 616–626 (2011). · DOI
  8. Sanchez, M. I. G. L. et al. RNA processing in human mitochondria. Cell Cycle 10, 2904–2916 (2011). · DOI
  9. Bhatta, A., Dienemann, C., Cramer, P. & Hillen, H. S. Structural basis of RNA processing by human mitochondrial RNase P. Nat. Struct. Mol. Biol. 28, 713–723 (2021). · DOI
  10. Vučković, A., Freyer, C., Wredenberg, A. & Hillen, H. S. The molecular machinery for maturation of primary mtDNA transcripts. Hum. Mol. Genet. 33, R19–R25 (2024). · DOI
  11. Vilardo, E. et al. A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase—extensive moonlighting in mitochondrial tRNA biogenesis. Nucleic Acids Res. 40, 11583–11593 (2012). · DOI
  12. Reinhard, L., Sridhara, S. & Hällberg, B. M. The MRPP1/MRPP2 complex is a tRNA-maturation platform in human mitochondria. Nucleic Acids Res. 45, gkx902 (2017). · DOI
  13. Bhatta, A. & Hillen, H. S. Structural and mechanistic basis of RNA processing by protein-only ribonuclease P enzymes. Trends Biochem. Sci. 47, 965–977 (2022). · DOI
  14. Dubin, D. T. Methylated nucleotide content of mitochondrial ribosomal RNA from hamster cells. J. Mol. Biol. 84, 257–273 (1974). · DOI
  15. Dubin, D. T. & Taylor, R. H. Modification of mitochondrial ribosomal RNA from hamster cells: the presence of GmG and late-methylated UmGmU in the large subunit (17 S) RNA. J. Mol. Biol. 121, 523–540 (1978). · DOI
  16. Dubin, D. T., Taylor, R. H. & Davenport, L. W. Methylation status of 13S ribosomal RNA from hamster mitochondria: the presence of a novel riboside, N 4 -methylcytidine. Nucleic Acids Res. 5, 4385–4398 (1978). · DOI
  17. Seidel-Rogol, B. L., McCulloch, V. & Shadel, G. S. Human mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loop. Nat. Genet 33, 23–24 (2002). · DOI
  18. Metodiev, M. D. et al. Methylation of 12S rRNA is necessary for in vivo stability of the small subunit of the mammalian mitochondrial ribosome. Cell Metab. 9, 386–397 (2009). · DOI
  19. Metodiev, M. D. et al. NSUN4 is a dual function mitochondrial protein required for both methylation of 12S rRNA and coordination of mitoribosomal assembly. PLoS Genet. 10, e1004110 (2014). · DOI
  20. Haute, L. V. et al. METTL15 introduces N4-methylcytidine into human mitochondrial 12S rRNA and is required for mitoribosome biogenesis. Nucleic Acids Res. 47, 10267–10281 (2019). · DOI
  21. Powell, C. A. & Minczuk, M. TRMT2B is responsible for both tRNA and rRNA m5U-methylation in human mitochondria. RNA Biol. 17, 451–462 (2020). · DOI
  22. Chen, H. et al. The human mitochondrial 12S rRNA m4C methyltransferase METTL15 is required for mitochondrial function. J. Biol. Chem. 295, 8505–8513 (2020). · DOI
  23. Singh, V. et al. Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk. Nat. Commun. 15, 4272 (2024). · DOI
  24. Lee, K.-W., Okot-Kotber, C., LaComb, J. F. & Bogenhagen, D. F. Mitochondrial Ribosomal RNA (rRNA) methyltransferase family members are positioned to modify nascent rRNA in foci near the mitochondrial DNA nucleoid*. J. Biol. Chem. 288, 31386–31399 (2013). · DOI
  25. Lee, K.-W. & Bogenhagen, D. F. Assignment of 2′-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA)*. J. Biol. Chem. 289, 24936–24942 (2014). · DOI
  26. Rorbach, J. et al. MRM2 and MRM3 are involved in biogenesis of the large subunit of the mitochondrial ribosome. Mol. Biol. Cell 25, 2542–2555 (2014). · DOI
  27. Bar-Yaacov, D. et al. Mitochondrial 16S rRNA is methylated by tRNA methyltransferase TRMT61B in all vertebrates. PLoS Biol. 14, e1002557 (2016). · DOI
  28. Zgadzay, Y. et al. Mettl15-Mettl17 modulates the transition from early to late pre-mitoribosome. bioRxiv 2024.12.18.629302 https://doi.org/10.1101/2024.12.18.629302 (2025). · DOI
  29. Mutti, C. D., Haute, L. V. & Minczuk, M. The catalytic activity of methyltransferase METTL15 is dispensable for its role in mitochondrial ribosome biogenesis. RNA Biol. 21, 687–694 (2024). · DOI
  30. Lai, C.-W. et al. FTSJ2, a heat shock-inducible mitochondrial protein, suppresses cell invasion and migration. PLoS ONE 9, e90818 (2014). · DOI
  31. Arai, T. et al. Single methylation of 23S rRNA triggers late steps of 50S ribosomal subunit assembly. Proc. Natl. Acad. Sci. USA 112, E4707–E4716 (2015). · DOI
  32. Wang, W. et al. Loss of a single methylation in 23S rRNA delays 50S assembly at multiple late stages and impairs translation initiation and elongation. Proc. Natl. Acad. Sci. USA 117, 15609–15619 (2020). · DOI
  33. Rebelo-Guiomar, P. et al. A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit. Nat. Commun. 13, 929 (2022). · DOI
  34. Agrimi, G. et al. Identification of the human mitochondrial S-adenosylmethionine transporter: bacterial expression, reconstitution, functional characterization and tissue distribution. Biochem. J. 379, 183–190 (2004). · DOI
  35. Palmieri, F., Scarcia, P. & Monné, M. Diseases caused by mutations in mitochondrial carrier genes SLC25: a review. Biomol 10, 655 (2020).
  36. Kunji, E. R. S., King, M. S., Ruprecht, J. J. & Thangaratnarajah, C. The SLC25 carrier family: important transport proteins in mitochondrial physiology and pathology. Physiology 35, 302–327 (2020). · DOI
  37. Kishita, Y. et al. Intra-mitochondrial methylation deficiency due to mutations in SLC25A26. Am. J. Hum. Genet. 97, 761–768 (2015). · DOI
  38. Ji, Y. et al. Identification and characterization of novel compound variants in SLC25A26 associated with combined oxidative phosphorylation deficiency 28. Gene 804, 145891 (2021). · DOI
  39. Rosenberger, F. A. et al. Pathogenic SLC25A26 variants impair SAH transport activity causing mitochondrial disease. Hum. Mol. Genet. 31, 2049–2062 (2022). · DOI
  40. Temperley, R. J., Wydro, M., Lightowlers, R. N. & Chrzanowska-Lightowlers, Z. M. Human mitochondrial mRNAs—like members of all families, similar but different. Biochim. Et. Biophys. Acta BBA Bioenerg. 1797, 1081–1085 (2010). · DOI
  41. Gustafsson, C. M., Falkenberg, M. & Larsson, N.-G. Maintenance and expression of mammalian mitochondrial DNA. Annu. Rev. Biochem. 85, 133–160 (2016). · DOI
  42. Antonicka, H., Weraarpachai, W., Vučković, A., Hillen, H. S. & Shoubridge, E. A. FASTKD5 processes mitochondrial pre-mRNAs at non-canonical cleavage sites. bioRxiv 2024.07.18.603998 https://doi.org/10.1101/2024.07.18.603998 (2024). · DOI
  43. Ohkubo, A. et al. The FASTK family proteins fine-tune mitochondrial RNA processing. PLoS Genet. 17, e1009873 (2021). · DOI
  44. Antonicka, H. & Shoubridge, E. A. Mitochondrial RNA granules are centers for posttranscriptional RNA processing and ribosome biogenesis. Cell Rep. 10, 920–932 (2015). · DOI
  45. Clemente, P. et al. ANGEL2 phosphatase activity is required for non-canonical mitochondrial RNA processing. Nat. Commun. 13, 5750 (2022). · DOI
  46. McShane, E. et al. A kinetic dichotomy between mitochondrial and nuclear gene expression processes. Mol. Cell 84, 1541–1555.e11 (2024). · DOI
  47. Ng, K. Y. et al. Nonstop mRNAs generate a ground state of mitochondrial gene expression noise. Sci. Adv. 8, eabq5234 (2022). · DOI
  48. Montoya, J., Christianson, T., Levens, D., Rabinowitz, M. & Attardi, G. Identification of initiation sites for heavy-strand and light-strand transcription in human mitochondrial DNA. Proc. Natl. Acad. Sci. USA 79, 7195–7199 (1982). · DOI
  49. Rackham, O. et al. Hierarchical RNA processing is required for mitochondrial ribosome assembly. Cell Rep. 16, 1874–1890 (2016). · DOI
  50. Chang, D. D. & Clayton, D. A. Identification of primary transcriptional start sites of mouse mitochondrial DNA: accurate in vitro initiation of both heavy- and light-strand transcripts. Mol. Cell Biol. 6, 1446–1453 (1986).
  51. Bonekamp, N. A. et al. Small-molecule inhibitors of human mitochondrial DNA transcription. Nature 588, 712–716 (2020). · DOI
  52. Lavdovskaia, E. et al. A roadmap for ribosome assembly in human mitochondria. Nat. Struct. Mol. Biol. 1–11 https://doi.org/10.1038/s41594-024-01356-w (2024). · DOI
  53. Greber, B. J. et al. The complete structure of the large subunit of the mammalian mitochondrial ribosome. Nature 515, 283–286 (2014). · DOI
  54. Brown, A. et al. Structure of the large ribosomal subunit from human mitochondria. Science 346, 718–722 (2014). · DOI
  55. Rorbach, J. et al. Human mitochondrial ribosomes can switch their structural RNA composition. Proc. Natl. Acad. Sci. USA 113, 12198–12201 (2016). · DOI
  56. Chandrasekaran, V. et al. Visualizing formation of the active site in the mitochondrial ribosome. eLife 10, e68806 (2021). · DOI
  57. Nguyen, T. G., Ritter, C. & Kummer, E. Structural insights into the role of GTPBP10 in the RNA maturation of the mitoribosome. Nat. Commun. 14, 7991 (2023). · DOI
  58. Cheng, J., Berninghausen, O. & Beckmann, R. A distinct assembly pathway of the human 39S late pre-mitoribosome. Nat. Commun. 12, 4544 (2021). · DOI
  59. Lavdovskaia, E., Hillen, H. S. & Richter-Dennerlein, R. Hierarchical folding of the catalytic core during mitochondrial ribosome biogenesis. Trends Cell Biol. 32, 182–185 (2022). · DOI
  60. Nikolay, R. et al. Snapshots of native pre-50S ribosomes reveal a biogenesis factor network and evolutionary specialization. Mol. Cell 81, 1200–1215.e9 (2021). · DOI
  61. Cipullo, M., Gesé, G. V., Khawaja, A., Hällberg, B. M. & Rorbach, J. Structural basis for late maturation steps of the human mitoribosomal large subunit. Nat. Commun. 12, 3673 (2021). · DOI
  62. Hillen, H. S. et al. Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling. Nat. Commun. 12, 3672 (2021). · DOI
  63. Khawaja, A., Cipullo, M., Krüger, A. & Rorbach, J. Insights into mitoribosomal biogenesis from recent structural studies. Trends Biochem. Sci. 48, 629–641 (2023). · DOI
  64. Cipullo, M. et al. Human GTPBP5 is involved in the late stage of mitoribosome large subunit assembly. Nucleic Acids Res. 49, gkaa1131 (2020).
  65. Lenarčič, T. et al. Stepwise maturation of the peptidyl transferase region of human mitoribosomes. Nat. Commun. 12, 3671 (2021). · DOI
  66. Temperley, R. J. et al. Investigation of a pathogenic mtDNA microdeletion reveals a translation-dependent deadenylation decay pathway in human mitochondria. Hum. Mol. Genet. 12, 2341–2348 (2003). · DOI
  67. Yelland, J. N., Bravo, J. P. K., Black, J. J., Taylor, D. W. & Johnson, A. W. A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome. Nat. Struct. Mol. Biol. 30, 91–98 (2023). · DOI
  68. Ishiguro, K., Arai, T. & Suzuki, T. Depletion of S-adenosylmethionine impacts on ribosome biogenesis through hypomodification of a single rRNA methylation. Nucleic Acids Res. 47, 4226–4239 (2019). · DOI
  69. Delaunay, S. et al. Mitochondrial RNA modifications shape metabolic plasticity in metastasis. Nature 607, 593–603 (2022). · DOI
  70. Bothe, G. W., Haspel, J. A., Smith, C. L., Wiener, H. H. & Burden, S. J. Selective expression of Cre recombinase in skeletal muscle fibers. Gene 26, 165 (2000).
  71. Li, H. New strategies to improve minimap2 alignment accuracy. Bioinformatics 37, 4572–4574 (2021). · DOI
  72. Danecek, P. et al. Twelve years of SAMtools and BCFtools. GigaScience 10, giab008 (2021). · DOI
  73. Quinlan, A. R. & Hall, I. M. BEDTools: a flexible suite of utilities for comparing genomic features. Bioinformatics 26, 841–842 (2010). · DOI · Paper page
  74. Li, X., Franz, T., Atanassov, I. & Colby, T. Proteomic profiling, methods and protocols. Methods Mol. Biol. 2261, 13–23 (2021). · DOI
  75. Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367–1372 (2008). · DOI · Paper page
  76. Ritchie, M. E. et al. limma powers differential expression analyses for RNA-sequencing and microarray studies. Nucleic Acids Res. 43, e47–e47 (2015). · DOI · Paper page
  77. Perez-Riverol, Y. et al. The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences. Nucleic Acids Res. 50, D543–D552 (2021). · DOI · Paper page
  78. Itoh, Y. et al. Mechanism of membrane-tethered mitochondrial protein synthesis. Science 371, 846–849 (2021). · DOI
  79. Charenton, C., Wilkinson, M. E. & Nagai, K. Mechanism of 5ʹ splice site transfer for human spliceosome activation. Science 364, 362–367 (2019). · DOI
  80. Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017). · DOI
  81. Zivanov, J., Nakane, T. & Scheres, S. H. W. Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION-3.1. IUCrJ 7, 253–267 (2020). · DOI
  82. Zhang, K. Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1–12 (2016). · DOI
  83. Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017). · DOI · Paper page
  84. Gese, G. V. & Hallberg, B. M. Human mitochondrial ribosome large subunit assembly intermediate with MTERF4-NSUN4, MRM2, MTG1 and the MALSU module. https://doi.org/10.2210/pdb7o9m/pdb (2021). · DOI
  85. Cheng, J., Berninghausen, O. & Beckmann, R. Cryo-EM structure of late human 39S mitoribosome assembly intermediates, state 1. https://doi.org/10.2210/pdb7oi6/pdb (2021). · DOI
  86. Pettersen, E. F. et al. UCSF Chimera—A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004). · DOI
  87. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. Sect. D. 66, 486–501 (2010). · DOI · Paper page
  88. Singh, V., Itoh, Y. & Amunts, A. Human mitochondrial ribosome at 2.2 A resolution (bound to partly built tRNAs and mRNA). https://doi.org/10.2210/pdb7qi4/pdb (2022). · DOI
  89. Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. Sect. D. 67, 235–242 (2011). · DOI · Paper page
  90. Liebschner, D. et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr. Sect. D. 75, 861–877 (2019). · DOI · Paper page
  91. Williams, C. J. et al. MolProbity: more and better reference data for improved all‐atom structure validation. Protein Sci. 27, 293–315 (2018). · DOI · Paper page

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Metadata

Authors
Glasgow, R. I. C., Singh, V., Peña-Pérez, L., Wilhalm, A., Moedas, M. F., Moore, D., Rosenberger, F. A., Li, X., Atanassov, I., Saba, M., Cipullo, M., Rorbach, J., Wedell, A., Freyer, C., Amunts, A., & Wredenberg, A.
Affiliations
  • Karolinska Institutet (SE)
  • Stockholm University (SE)
  • Karolinska University Hospital (SE)
  • Max Planck Institute for Biology of Ageing (DE)
  • University of Münster (DE)
Corresponding author
  • Freyer, Christoph
  • Amunts, Alexey
  • Wredenberg, Anna
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2025-06-25
Volume
16
Issue
1
Pages
5388-5388
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-025-60977-x
PMC
PMC12198368
OpenAlex
W4411622405
Cited by
14
References
6
Citations by year
2026: 9 · 2025: 5
FWCI
4.18
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
  • Cancerfonden (RS2022-0708, 21 1621 Pj, VR2022-01287, 2-190/2022, KAW2019.0109, NN0082202)
  • Karolinska Institutet (2-190/2022)
  • Knut och Alice Wallenbergs Stiftelse (KAW 2019.0109, KAW2019)
  • Vetenskapsrådet (2-190/2022, RS2022-0708, 07091, 2023-07091, NN0082202, 2022-01287, 2018-, 21 1621 Pj, KAW2019.0109)
  • Stockholms Universitet
  • Science for Life Laboratory
  • Novo Nordisk Foundation Center for Basic Metabolic Research (NN0082202)
  • Uppsala Multidisciplinary Center for Advanced Computational Science
  • H2020 European Research Council (805230)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords
S-adenosylmethionine, mitochondrial ribosome biogenesis, SAM-dependent methylation, peptidyl transferase center, mitochondrial translation, mitochondrial gene expression, RNA methylation
MeSH terms
Mitochondrial Ribosomes, Animals, Fibroblasts, Methylation, Mitochondria, Ribosomal Proteins, RNA Processing, Post-Transcriptional, S-Adenosylmethionine, Cryoelectron Microscopy, Mitochondrial Proteins, Proteomics, Mice

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