CoChat
Sign Up
Cited by 3RNA modifications and cancerDNA and Nucleic Acid ChemistryRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

A single viral enzyme drives tRNA-dependent hypermodification of DNA at adenine

Open access
Silva, Rebekah M. B., Slyvka, Anton, Lee, Yan-Jiun, Guan, Chudi, Lund, Sean R., Raleigh, Elisabeth A., Skowronek, Krzysztof, Kuska, Michael S., Bochtler, Matthias, Weigele, Peter R.·2026·Nature Communications
DOI 10.1038/s41467-026-70671-1PMC PMC13219725

Published version of a preprint

Open this paper in CoChat — free accountOpen PDF

Abstract

Abstract Bacteriophage enzymes synthesize varied and complex DNA hypermodifications. The enzyme encoded by the phage Mu gene mom is necessary for post-replicative carbamoylmethyl addition to the exocyclic amine of deoxyadenosine in DNA during the lytic phase of the viral life-cycle. The molecular details of this modification reaction, including the molecular origins of the modification itself, have long eluded understanding. Here, we demonstrate that Mom co-opts the translational machinery of the host by harvesting activated glycine from charged tRNA Gly to hypermodify adenine. Based on this insight, we report the first in vitro reconstitution of the Mu hypermodification from purified components. Using isotope labeling, we demonstrate that the carbamoyl nitrogen of the Mom modification is derived from the N 6 of adenine, indicating an on-base rearrangement of the N 6 aminoacylation product, possibly via a cyclic intermediate. Informed by the X-ray crystal structure of Mom, we have probed the location of the active site, identified a novel insertion, and established substrate specificities of the Mom enzyme.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/s41467-026-70671-1

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 120

  1. Isaev, A. B., Musharova, O. S. & Severinov, K. V. Microbial arsenal of antiviral defenses—part I. Biochemistry. 86, 319–337 (2021).
  2. Isaev, A. B., Musharova, O. S. & Severinov, K. V. Microbial arsenal of antiviral defenses. Part II. Biochemistry. 86, 449–470 (2021).
  3. Hall, R. H. N6-(δ2-Isopentenyl)adenosine: chemical reactions, biosynthesis, metabolism, and significance to the structure and function of †RNA. Prog. Nucleic Acid Res. 10, 57–86 (1970). · DOI
  4. Warren, R. A. J. Modified bases in bacteriophage DNAs. Annu. Rev. Microbiol. 34, 137–158 (1980). · DOI
  5. Gommers-Ampt, J. H. & Borst, P. Hypermodified bases in DNA. FASEB J. 9, 1034–1042 (1995). · DOI
  6. Weigele, P. & Raleigh, E. A. Biosynthesis and function of modified bases in bacteria and their viruses. Chem. Rev. 116, 12655–12687 (2016). · DOI
  7. Parker, M. J., Lee, Y.-J., Weigele, P. R. & Saleh, L. 5-Methylpyrimidines and their modifications in DNA. In Comprehensive Natural Products III 465–488 (Elsevier, 2020). · DOI
  8. Hutinet, G., Lee, Y.-J., de Crécy-Lagard, V. & Weigele, P. R. Hypermodified DNA in viruses of E. coli and Salmonella. EcoSal Plus. 9, eESP-0028-2019 (2021). · DOI
  9. Flodman, K. et al. Type II restriction of bacteriophage DNA with 5hmdU-derived base modifications. Front. Microbiol. 10, 584 (2019). · DOI
  10. Flodman, K., Corrêa, I. R., Dai, N., Weigele, P. & Xu, S. In vitro type II restriction of bacteriophage DNA with modified pyrimidines. Front. Microbiol. 11, 604618 (2020). · DOI
  11. Hall, R. H. The Modified Nucleosides in Nucleic Acids. (Columbia University Press, 1971).
  12. Galburt, E. A., Pelletier, J., Wilson, G. & Stoddard, B. L. Structure of a tRNA repair enzyme and molecular biology workhorse T4 polynucleotide kinase. Structure. 10, 1249–1260 (2002). · DOI
  13. Shuman, S. DNA ligases: progress and prospects*. J. Biol. Chem. 284, 17365–17369 (2009). · DOI
  14. Doudna, J. A. & Charpentier, E. The new frontier of genome engineering with CRISPR-Cas9. Science. 346, 1258096 (2014). · DOI · Paper page
  15. Allet, B. & Bukhari, A. I. Analysis of bacteriophage Mu and λ-Mu hybrid DNAs by specific endonucleases. J. Mol. Biol. 92, 529–540 (1975). · DOI
  16. Toussaint, A. The DNA modification function of temperate phage Mu-1. Virology 70, 17–27 (1976). · DOI
  17. Hattman, S. Unusual modification of bacteriophage Mu DNA. J. Virol. 32, 468–475 (1979). · DOI
  18. Khatoon, H. & Bukhari, A. I. Bacteriophage Mu-induced modification of DNA is dependent upon a host function. J. Bacteriol. 136, 423–428 (1978). · DOI
  19. Hattman, S. Specificity of the bacteriophage Mu mom+ -controlled DNA modification. J. Virol. 34, 277–279 (1980). · DOI
  20. Swinton, D. et al. Purification and characterization of the unusual deoxynucleoside, a-N-(9-fi-D-2’-deoxyribofuranosylpurin-6-yl)glycinamide, specified. Proc. Natl. Acad. Sci. USA 80, 7400–7404 (1983). · DOI
  21. Toussaint, A. My life with Mu. Bacteriophage. 5, e1034336 (2015). · DOI
  22. Karambelkar, S. et al. Emergence of a novel immune-evasion strategy from an ancestral protein fold in bacteriophage Mu. Nucleic Acids Res. 48, 5294–5305 (2020). · DOI
  23. Newton, R. P., Kingston, E. E. & Overton, A. Identification of novel nucleotides found in the red seaweed Porphyra umbilicalis. Rapid Commun. Mass Spectrom. 9, 305–311 (1995). · DOI
  24. Strzelecka, D., Chmielinski, S., Bednarek, S., Jemielity, J. & Kowalska, J. Analysis of mononucleotides by tandem mass spectrometry: investigation of fragmentation pathways for phosphate- and ribose-modified nucleotide analogues. Sci. Rep. 7, 8931 (2017). · DOI
  25. Kahmann, R., Seiler, A., Wulczyn, F. G. & Pfaff, E. The mom gene of bacteriophage Mu: a unique regulatory scheme to control a lethal function. Gene. 39, 61–70 (1985). · DOI
  26. Krüger, D. H. & Bickle, T. A. Bacteriophage survival: multiple mechanisms for avoiding the deoxyribonucleic acid restriction systems of their hosts. Microbiol. Rev. 47, 345–360 (1983). · DOI
  27. Kaminska, K. H. & Bujnicki, J. M. Bacteriophage Mu Mom protein responsible for DNA modification is a new member of the acyltransferase superfamily. Cell Cycle. 7, 120–121 (2008). · DOI
  28. Iyer, L. M., Tahiliani, M., Rao, A. & Aravind, L. Prediction of novel families of enzymes involved in oxidative and other complex modifications of bases in nucleic acids. Cell Cycle. 8, 1698–1710 (2009). · DOI
  29. Iyer, L. M., Zhang, D. & Aravind, L. Adenine methylation in eukaryotes: apprehending the complex evolutionary history and functional potential of an epigenetic modification. Bioessays. 38, 27–40 (2016). · DOI
  30. Iyer, L. M., Anantharaman, V., Krishnan, A., Burroughs, A. M. & Aravind, L. Jumbo phages: a comparative genomic overview of core functions and adaptions for biological conflicts. Viruses. 13, 63 (2021). · DOI
  31. Lee, Y.-J. et al. Identification and biosynthesis of thymidine hypermodifications in the genomic DNA of widespread bacterial viruses. Proc. Natl. Acad. Sci. USA. 115, E3116–E3125 (2018).
  32. Lee, Y.-J. et al. Pathways of thymidine hypermodification. Nucleic Acids Res. 50, 3001–3017 (2021). · DOI
  33. Shimizu, Y. & Ueda, T. Cell-free protein production, methods and protocols. Methods Mol. Biol. 607, 11–21 (2009). · DOI
  34. Tuckey, C., Asahara, H., Zhou, Y. & Chong, S. Protein synthesis using a reconstituted cell-free system. Curr. Protoc. Mol. Biol. 108, 16.31.1–16.31.22 (2014). · DOI
  35. Burckhardt, R. M. & Escalante-Semerena, J. C. Small-molecule acetylation by GCN5-related N-acetyltransferases in bacteria. Microbiol. Mol. Biol. R 84, https://doi.org/10.1128/mmbr.00090-19 (2020). · DOI
  36. Favrot, L., Blanchard, J. S. & Vergnolle, O. Bacterial GCN5-related N-acetyltransferases: from resistance to regulation. Biochemistry. 55, 989–1002 (2016). · DOI
  37. Baumgartner, J. T. et al. Gcn5-related N-acetyltransferases (GNATs) with a catalytic serine residue can play ping-pong too. Front. Mol. Biosci. 8, 646046 (2021). · DOI
  38. Ostrem, D. L. & Berg, P. Glycyl transfer ribonucleic acid synthetase from Escherichia coli: purification, properties, and substrate binding. Biochemistry 13, 1338–1348 (1974). · DOI
  39. Toth, M. J. & Schimmel, P. Deletions in the large (beta) subunit of a hetero-oligomeric aminoacyl-tRNA synthetase. J. Biol. Chem. 265, 1000–1004 (1990). · DOI
  40. Valencia-Sánchez, M. I. et al. Structural insights into the polyphyletic origins of glycyl tRNA synthetases. J. Biol. Chem. 291, 14430–14446 (2016). · DOI
  41. Gomez, M. A. R. & Ibba, M. Aminoacyl-tRNA synthetases. RNA 26, rna.071720.119 (2020).
  42. Ju, Y. et al. X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications. Nucleic Acids Res. 49, 10106–10119 (2021). · DOI
  43. Grünberg, S. et al. Enhanced expression and purification of nucleotide-specific ribonucleases MC1 and Cusativin. Protein Expr. Purif. 190, 105987 (2022). · DOI
  44. Wolf, E. J. et al. Human RNase 4 improves mRNA sequence characterization by LC–MS/MS. Nucleic Acids Res. 50, e106–e106 (2022). · DOI
  45. Wolf, E. J., Dai, N., Chan, S.-H. & Corrêa, I. R. Selective characterization of mRNA 5′ end-capping by DNA probe-directed enrichment with site-specific endoribonucleases. ACS Pharmacol. Transl. Sci. 6, 1692–1702 (2023). · DOI
  46. Sprinzl, M. & Cramer, F. Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2’- or 3’-hydroxyl group of the terminal adenosine. Proc. Natl. Acad. Sci. USA. 72, 3049–3053 (1975). · DOI
  47. Asahara, H. & Uhlenbeck, O. C. The tRNA specificity of thermus thermophilus EF-Tu. Proc. Natl. Acad. Sci. USA. 99, 3499–3504 (2002). · DOI
  48. Walker, S. E. & Fredrick, K. Preparation and evaluation of acylated tRNAs. Methods. 44, 81–86 (2008). · DOI
  49. Gamper, H. & Hou, Y.-M. A label-free assay for aminoacylation of tRNA. Genes 11, 1173 (2020). · DOI
  50. Xu, X. et al. MenT nucleotidyltransferase toxins extend tRNA acceptor stems and can be inhibited by asymmetrical antitoxin binding. Nat. Commun. 14, 4644 (2023). · DOI
  51. Chan, P. P. & Lowe, T. M. GtRNAdb: a database of transfer RNA genes detected in genomic sequence. Nucleic Acids Res. 37, D93–D97 (2009). · DOI
  52. Chan, P. P. & Lowe, T. M. GtRNAdb 2.0: an expanded database of transfer RNA genes identified in complete and draft genomes. Nucleic Acids Res. 44, D184–D189 (2016). · DOI
  53. Leiva, L. E. et al. Modulation of Escherichia coli translation by the specific inactivation of tRNAGly under oxidative stress. Front. Genet. 11, 856 (2020). · DOI
  54. Stewart, T. S., Roberts, R. J. & Strominger, J. L. Novel species of tRNA. Nature. 230, 36–38 (1971). · DOI
  55. Roberts, R. J. Structures of two glycyl-tRNAs from Staphylococcus epidermidis. Nat. N. Biol. 237, 44–45 (1972). · DOI
  56. Beebe, K., de Pouplana, L. R. & Schimmel, P. Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 22, 668–675 (2003). · DOI
  57. Pasman, Z. et al. Substrate specificity and catalysis by the editing active site of alanyl-tRNA synthetase from Escherichia coli. Biochemistry. 50, 1474–1482 (2011). · DOI
  58. Kavoor, A., Kelly, P. & Ibba, M. Escherichia coli alanyl-tRNA synthetase maintains proofreading activity and translational accuracy under oxidative stress. J. Biol. Chem. 298, 101601 (2022). · DOI
  59. Fonvielle, M. et al. Aminoacyl-tRNA recognition by the FemX Wv transferase for bacterial cell wall synthesis. Nucleic Acids Res. 37, 1589–1601 (2009). · DOI
  60. Villet, R. et al. Idiosyncratic features in tRNAs participating in bacterial cell wall synthesis. Nucleic Acids Res. 35, 6870–6883 (2007). · DOI
  61. Bikmetov, D. et al. GNAT toxins evolve toward narrow tRNA target specificities. Nucleic Acids Res. 50, 5807–5817 (2022). · DOI
  62. Vetting, M. W. et al. Structure and functions of the GNAT superfamily of acetyltransferases. Arch. Biochem. Biophys. 433, 212–226 (2005). · DOI
  63. Ud-Din, A. I. M. S., Tikhomirova, A. & Roujeinikova, A. Structure and functional diversity of GCN5-related N-acetyltransferases (GNAT). Int. J. Mol. Sci. 17, 1018 (2016). · DOI
  64. Bochtler, M. & Fernandes, H. DNA adenine methylation in eukaryotes: enzymatic mark or a form of DNA damage? Bioessays 43, 2000243 (2021). · DOI
  65. Fu, D., Calvo, J. A. & Samson, L. D. Balancing repair and tolerance of DNA damage caused by alkylating agents. Nat. Rev. Cancer. 12, 104–120 (2012). · DOI
  66. Xu, G.-L. & Bochtler, M. Reversal of nucleobase methylation by dioxygenases. Nat. Chem. Biol. 16, 1160–1169 (2020). · DOI
  67. Macon, J. B. & Wolfenden, R. 1-Methyladenosine. Dimroth rearrangement and reversible reduction. Biochemistry. 7, 3453–3458 (1968). · DOI
  68. Ashry, E. S. H. E., Nadeem, S., Shah, M. R. & Kilany, Y. E. Chapter 5- Recent advances in the Dimroth rearrangement: a valuable tool for the synthesis of heterocycles. Advances in Heterocyclic Chemistry 101, 161–228 (Academic Press, 2010). · DOI
  69. Neese, F., Wennmohs, F., Becker, U. & Riplinger, C. The ORCA quantum chemistry program package. J. Chem. Phys. 152, 224108 (2020). · DOI
  70. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007). · DOI · Paper page
  71. 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
  72. Holm, L. Dali server: structural unification of protein families. Nucleic Acids Res. 50, W210–W215 (2022). · DOI
  73. Laskowski, R. A., Jabłońska, J., Pravda, L., Vařeková, R. S. & Thornton, J. M. PDBsum: structural summaries of PDB entries. Protein Sci. Publ. Protein Soc. 27, 129–134 (2018). · DOI
  74. Cheverton, A. M. et al. A Salmonella toxin promotes persister formation through acetylation of tRNA. Mol. Cell. 63, 86–96 (2016). · DOI
  75. Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774–797 (2007). · DOI
  76. Yashiro, Y., Zhang, C., Sakaguchi, Y., Suzuki, T. & Tomita, K. Molecular basis of glycyl-tRNAGly acetylation by TacT from Salmonella typhimurium. Cell Rep. 37, 110130 (2021). · DOI
  77. Hall, R. H. Isolation of N 6 -(Aminoacyl)adenosine from Yeast Ribonucleic Acid. Biochemistry 3, 769–773 (1964). · DOI
  78. Chheda, G. B. & Hall, R. H. Aminoacyl nucleosides. III. A novel rearangement: conversion of N6-(α-Aminoacyl) adenines into N-(6-Purinyl)amino Acids. Biochemistry. 5, 2082–2091 (1966). · DOI
  79. Chheda, G. B., Hall, R. H. & Tanna, P. M. Aminoacyl nucleosides. V. Mechanism of the rearrangement of N6-(α-aminoacyl)adenines into N-(6-purinyl)amino acids. J. Org. Chem. 34, 3498–3502 (1969). · DOI
  80. Masurier, N. et al. Synthesis of peptide-adenine conjugates as a new tool for monitoring protease activity. Eur. J. Org. Chem. 2019, 176–183 (2018). · DOI
  81. Lindahl, T. Instability and decay of the primary structure of DNA. Nature 362, 709–715 (1993). · DOI · Paper page
  82. Moutiez, M., Belin, P. & Gondry, M. Aminoacyl-tRNA-utilizing enzymes in natural product biosynthesis. Chem. Rev. 117, 5578–5618 (2017). · DOI
  83. Hattman, S. Unusual transcriptional and translational regulation of the bacteriophage Mu mom operon. Pharmacol. Ther. 84, 367–388 (1999). · DOI
  84. Chimnaronk, S. et al. RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon. EMBO J. 28, 1362–1373 (2009). · DOI
  85. Huang, B., Johansson, M. J. O. & Byström, A. S. An early step in wobble uridine tRNA modification requires the Elongator complex. RNA. 11, 424–436 (2005). · DOI
  86. Dauden, M. I. et al. Architecture of the yeast Elongator complex. EMBO Rep. 18, 264–279 (2017). · DOI
  87. Lee, Y.-J. & Weigele, P. R. Detection of modified bases in bacteriophage genomic DNA. Methods Mol. Biol. 2198, 53–66 (2020). · DOI
  88. Li, D., Liu, C.-M., Luo, R., Sadakane, K. & Lam, T.-W. MEGAHIT: an ultra-fast single-node solution for large and complex metagenomics assembly via succinct de Bruijn graph. Bioinformatics 31, 1674–1676 (2015). · DOI
  89. Parker, M. J., Weigele, P. R. & Saleh, L. Insights into the biochemistry, evolution, and biotechnological applications of the ten-eleven translocation (TET) enzymes. Biochemistry. 58, 450–467 (2019). · DOI
  90. Burke, E. J. et al. Phage-encoded ten-eleven translocation dioxygenase (TET) is active in C5-cytosine hypermodification in DNA. Proc. Natl. Acad. Sci. USA 118, e2026742118 (2021). · DOI
  91. Cavaluzzi, M. J. & Borer, P. N. Revised UV extinction coefficients for nucleoside-5′-monophosphates and unpaired DNA and RNA. Nucleic Acids Res. 32, e13–e13 (2004). · DOI
  92. Dunn, D. B. & Hall, R. H. Handbook of Biochemistry and Molecular Biology 269–358 (C.R.C. Press, 2010). · DOI
  93. Francois, C. J. L., Jang, Y. H., Cagin, T., Goddard, W. A. & Sowers, L. C. Conformation and proton configuration of pyrimidine deoxynucleoside oxidation damage products in water. Chem. Res Toxicol. 13, 462–470 (2000). · DOI
  94. Milo, R., Jorgensen, P., Moran, U., Weber, G. & Springer, M. BioNumbers—the database of key numbers in molecular and cell biology. Nucleic Acids Res. 38, D750–D753 (2010). · DOI · Paper page
  95. Edwards, A. L., Garst, A. D. & Batey, R. T. Determining structures of RNA aptamers and riboswitches by X-ray crystallography. Methods Mol. Biol. 535, 135–163 (2009). · DOI
  96. Quinlivan, E. P. & Gregory, J. F. DNA digestion to deoxyribonucleoside: a simplified one-step procedure. Anal. Biochem. 373, 383–385 (2008). · DOI
  97. Sprinzl, M., Sternbach, H., Haar, F. V. D. & Cramer, F. Enzymatic Incorporation of ATP and CTP analogues into the 3′ End of tRNA. Eur. J. Biochem. 81, 579–589 (1977). · DOI
  98. Katoh, T. & Suga, H. Flexizyme-catalyzed synthesis of 3′-aminoacyl-NH-tRNAs. Nucleic Acids Res. 47, e54 (2019). · DOI
  99. Kent, A. D. et al. Thioesters support efficient protein biosynthesis by the ribosome. ACS Cent. Sci. 11, 404–412 (2025). · DOI
  100. Krug, M., Weiss, M. S., Heinemann, U. & Mueller, U. XDSAPP: a graphical user interface for the convenient processing of diffraction data using XDS. J. Appl. Crystallogr. 45, 568–572 (2012). · DOI
  101. 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
  102. Pettersen, E. F. et al. UCSF ChimeraX: structure visualization for researchers, educators, and developers. Protein Sci. 30, 70–82 (2020). · DOI
  103. Gibrat, J.-F., Madej, T. & Bryant, S. H. Surprising similarities in structure comparison. Curr. Opin. Struct. Biol. 6, 377–385 (1996). · DOI
  104. Eddy, S. R. Accelerated profile HMM searches. PLoS Comput. Biol. 7, e1002195 (2011). · DOI · Paper page
  105. Paez-Espino, D. et al. IMG/VR v.2.0: an integrated data management and analysis system for cultivated and environmental viral genomes. Nucleic Acids Res. 47, D678–D686 (2019). · DOI
  106. Gregory, A. C. et al. Marine DNA viral macro- and microdiversity from pole to pole. Cell. 177, 1109–1123.e14 (2019). · DOI
  107. Seemann, T. Prokka: rapid prokaryotic genome annotation. Bioinformatics 30, 2068–2069 (2014). · DOI
  108. Arkin, A. P. et al. KBase: the United States Department of Energy Systems Biology Knowledgebase. Nat. Biotechnol. 36, 566–569 (2018). · DOI
  109. El-Gebali, S. et al. The Pfam protein families database in 2019. Nucleic Acids Res. 47, D427–D432 (2019). · DOI · Paper page
  110. Gerlt, J. A. et al. Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): a web tool for generating protein sequence similarity networks. Biochim. Biophys. Acta Proteins Proteom. 1854, 1019–1037 (2015). · DOI
  111. O’Toole, K. H., Imperiali, B. & Allen, K. N. Glycoconjugate pathway connections revealed by sequence similarity network analysis of the monotopic phosphoglycosyl transferases. Proc. Natl. Acad. Sci. USA 118, e2018289118 (2021). · DOI
  112. Shannon, P. et al. Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 13, 2498–2504 (2003). · DOI · Paper page
  113. Mirdita, M. et al. ColabFold: making protein folding accessible to all. Nat. Methods 19, 679–682 (2022). · DOI · Paper page
  114. Francklyn, C. S. & Minajigi, A. tRNA as an active chemical scaffold for diverse chemical transformations. FEBS Lett. 584, 366–375 (2010). · DOI
  115. Ulrich, E. C. & Donk, W. A. van der. Cameo appearances of aminoacyl-tRNA in natural product biosynthesis. Curr. Opin. Chem. Biol. 35, 29–36 (2016). · DOI
  116. Su, Z., Wilson, B., Kumar, P. & Dutta, A. Noncanonical roles of tRNAs: tRNA fragments and beyond. Annu. Rev. Genet. 54, 1–23 (2020). · DOI
  117. Maruyama, C. & Hamano, Y. tRNA-dependent amide bond–forming enzymes in peptide natural product biosynthesis. Curr. Opin. Chem. Biol. 59, 164–171 (2020). · DOI
  118. Hentchel, K. L. & Escalante-Semerena, J. C. Acylation of biomolecules in prokaryotes: a widespread strategy for the control of biological function and metabolic stress. Microbiol. Mol. Biol. R. 79, 321–346 (2015). · DOI
  119. Yashiro, Y., Sakaguchi, Y., Suzuki, T. & Tomita, K. Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli. Nat. Commun. 11, 5438 (2020). · DOI
  120. Skiba, M. A. et al. Repurposing the GNAT fold in the initiation of polyketide biosynthesis. Structure. 28, 63–74.e4 (2020). · DOI

Metadata

Authors
Silva, R. M. B., Slyvka, A., Lee, Y.-J., Guan, C., Lund, S. R., Raleigh, E. A., Skowronek, K., Kuska, M. S., Bochtler, M., & Weigele, P. R.
Affiliations
  • New England Biolabs (United States) (US)
  • International Institute of Molecular and Cell Biology (PL)
Corresponding author
  • Bochtler, Matthias
  • Weigele, Peter R.
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2026-04-03
Volume
17
Issue
1
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-026-70671-1
PMC
PMC13219725
OpenAlex
W7148737707
Cited by
3
References
2
FWCI
0.00
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • New England Biolabs
  • Fundacja na rzecz Nauki Polskiej (FNP, POIR.04.04.00-00-5D81/17-00)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
N6-methyladenosine, GNAT superfamily, acetyltransferase, catalytic residues
MeSH terms
Adenine, Deoxyadenosines, DNA, Viral, Models, Molecular, Bacteriophage mu, RNA, Transfer, Viral Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review