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Since eukaryotes are not able to synthesize queuosine de novo, they have to salvage queuine (the queuosine base) as a micronutrient from food and\/or the gut microbiome. The heterodimeric Zn2+ containing enzyme tRNA-guanine transglycosylase (TGT) catalyzes the insertion of queuine into the above-named tRNAs in exchange for the genetically encoded guanine. This enzyme has attracted medical interest since it was shown to be potentially useful for the treatment of multiple sclerosis. In addition, TGT inactivation via gene knockout leads to the suppressed cell proliferation and migration of certain breast cancer cells, which may render this enzyme a potential target for the design of compounds supporting breast cancer therapy. As a prerequisite to fully exploit the medical potential of eukaryotic TGT, we have determined and analyzed a number of crystal structures of the functional murine TGT with and without bound queuine. In addition, we have investigated the importance of two residues of its non-catalytic subunit on dimer stability and determined the Michaelis\u2013Menten parameters of murine TGT with respect to tRNA and several natural and artificial nucleobase substrates. Ultimately, on the basis of available TGT crystal structures, we provide an entirely conclusive reaction mechanism for this enzyme, which in detail explains why the TGT-catalyzed insertion of some nucleobases into tRNA occurs reversibly while that of others is irreversible.<\/jats:p>","DOI":"10.1021\/acschembio.2c00368","type":"journal-article","created":{"date-parts":[[2022,7,11]],"date-time":"2022-07-11T08:45:06Z","timestamp":1657529106000},"page":"2229-2247","source":"Crossref","is-referenced-by-count":14,"title":["Structural and\nBiochemical Investigation of the Heterodimeric\nMurine tRNA-Guanine Transglycosylase"],"prefix":"10.1021","volume":"17","author":[{"given":"Maurice","family":"Sebastiani","sequence":"first","affiliation":[{"name":"Philipps-Universita\u0308t Marburg , , Marbacher Weg 8 , ,","place":["Marburg, Germany, D-35037"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christina","family":"Behrens","sequence":"additional","affiliation":[{"name":"Philipps-Universita\u0308t Marburg , , Marbacher Weg 8 , ,","place":["Marburg, Germany, D-35037"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefanie","family":"Do\u0308rr","sequence":"additional","affiliation":[{"name":"Philipps-Universita\u0308t Marburg , , Marbacher Weg 8 , ,","place":["Marburg, Germany, D-35037"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6729-6027","authenticated-orcid":true,"given":"Hans-Dieter","family":"Gerber","sequence":"additional","affiliation":[{"name":"Philipps-Universita\u0308t Marburg , , Marbacher Weg 8 , ,","place":["Marburg, Germany, D-35037"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rania","family":"Benazza","sequence":"additional","affiliation":[{"name":"Laboratoire de Spectrome\u0301trie de Masse BioOrganique, Universite\u0301 de Strasbourg, CNRS, IPHC UMR 7178 , ,","place":["F-Strasbourg, France, 67000"]},{"name":"Infrastructure Nationale de Prote\u0301omique ProFI\ue5f8FR2048 , ,","place":["Strasbourg, France, 67087"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oscar","family":"Hernandez-Alba","sequence":"additional","affiliation":[{"name":"Laboratoire de Spectrome\u0301trie de Masse BioOrganique, Universite\u0301 de Strasbourg, CNRS, IPHC UMR 7178 , ,","place":["F-Strasbourg, France, 67000"]},{"name":"Infrastructure Nationale de Prote\u0301omique ProFI\ue5f8FR2048 , ,","place":["Strasbourg, France, 67087"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4013-4129","authenticated-orcid":true,"given":"Sarah","family":"Cianfe\u0301rani","sequence":"additional","affiliation":[{"name":"Laboratoire de Spectrome\u0301trie de Masse BioOrganique, Universite\u0301 de Strasbourg, CNRS, IPHC UMR 7178 , ,","place":["F-Strasbourg, France, 67000"]},{"name":"Infrastructure Nationale de Prote\u0301omique ProFI\ue5f8FR2048 , ,","place":["Strasbourg, France, 67087"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4913-390X","authenticated-orcid":true,"given":"Gerhard","family":"Klebe","sequence":"additional","affiliation":[{"name":"Philipps-Universita\u0308t Marburg , , Marbacher Weg 8 , ,","place":["Marburg, Germany, D-35037"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreas","family":"Heine","sequence":"additional","affiliation":[{"name":"Philipps-Universita\u0308t Marburg , , Marbacher Weg 8 , ,","place":["Marburg, Germany, D-35037"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3673-7971","authenticated-orcid":true,"given":"Klaus","family":"Reuter","sequence":"additional","affiliation":[{"name":"Philipps-Universita\u0308t Marburg , , Marbacher Weg 8 , ,","place":["Marburg, Germany, D-35037"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2022,7,11]]},"reference":[{"key":"2026081413085818800_cit1","doi-asserted-by":"publisher","DOI":"10.15252\/embj.201899777","article-title":"Queuosine-modified tRNAs confer nutritional\ncontrol of protein translation","volume":"37","author":"Tuorto","year":"2018","journal-title":"EMBO J."},{"key":"2026081413085818800_cit2","doi-asserted-by":"publisher","first-page":"1305","DOI":"10.1261\/rna.067033.118","article-title":"Queuosine modification\nprotects cognate tRNAs against ribonuclease cleavage","volume":"24","author":"Wang","year":"2018","journal-title":"RNA"},{"key":"2026081413085818800_cit3","doi-asserted-by":"publisher","first-page":"10952","DOI":"10.1093\/nar\/gkv980","article-title":"Dynamic\nmodulation of Dnmt2-dependent tRNA methylation\nby the micronutrient queuine","volume":"43","author":"Mu\u0308ller","year":"2015","journal-title":"Nucleic Acids\nRes."},{"key":"2026081413085818800_cit4","doi-asserted-by":"publisher","first-page":"7876","DOI":"10.1128\/jb.00874-08","article-title":"Biosynthesis of 7-deazaguanosine-modified\ntRNA nucleosides: a new role for GTP cyclohydrolase I","volume":"190","author":"Phillips","year":"2008","journal-title":"J. Bacteriol."},{"key":"2026081413085818800_cit5","doi-asserted-by":"publisher","first-page":"2301","DOI":"10.1021\/bi9001437","article-title":"Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin\nsynthase","volume":"48","author":"McCarty","year":"2009","journal-title":"Biochemistry"},{"key":"2026081413085818800_cit6","doi-asserted-by":"publisher","first-page":"3847","DOI":"10.1021\/bi900400e","article-title":"The deazapurine\nbiosynthetic pathway revealed: in vitro enzymatic synthesis of preQ0 from guanosin 5\u2032-triphosphate in four steps","volume":"48","author":"McCarty","year":"2009","journal-title":"Biochemistry"},{"key":"2026081413085818800_cit7","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1021\/bi301156w","article-title":"Spectroscopic,\nsteady-state kinetic,\nand mechanistic characterization of the radical SAM enzyme QueE, which\ncatalyzes a complex cyclization reaction in the biosynthesis of 7-deazapurines","volume":"52","author":"McCarty","year":"2013","journal-title":"Biochemistry"},{"key":"2026081413085818800_cit8","doi-asserted-by":"publisher","first-page":"4264","DOI":"10.1073\/pnas.0408056102","article-title":"From cyclohydrolase to oxidoreductase: discovery of\nnitrile reductase activity in a common fold","volume":"102","author":"Van\nLanen","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081413085818800_cit9","doi-asserted-by":"publisher","first-page":"3061","DOI":"10.1016\/s0021-9258(17)30182-5","article-title":"Isolation and characterization of a guanine insertion\nenzyme, a specific tRNA transglycosylase, from Escherichia coli","volume":"254","author":"Okada","year":"1979","journal-title":"J. Biol. Chem."},{"key":"2026081413085818800_cit10","doi-asserted-by":"publisher","first-page":"10491","DOI":"10.1074\/jbc.m207727200","article-title":"tRNA modification by S-adenosylmethionine:tRNA\nribosyltransferase-isomerase","volume":"278","author":"Van\nLanen","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2026081413085818800_cit11","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1016\/j.bbrc.2006.10.096","article-title":"Crystal structure of Bacillus subtilis\nS-adenosylmethionine:tRNA\nribosyl transferase-isomerase","volume":"351","author":"Grimm","year":"2006","journal-title":"Biochem. Biophys.\nRes. 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Struct. Mol. Biol."},{"key":"2026081413085818800_cit16","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1016\/j.jmb.2009.07.040","article-title":"An integrative approach\ncombining\nnoncovalent mass spectrometry, enzyme kinetics and X-ray crystallography\nto decipher Tgt protein-protein and protein-RNA interaction","volume":"393","author":"Ritschel","year":"2009","journal-title":"J. Mol. Biol."},{"key":"2026081413085818800_cit17","doi-asserted-by":"publisher","first-page":"18218","DOI":"10.1074\/jbc.m109.002477","article-title":"Queuosine formation in eukaryotic\ntRNA occurs via a\nmitochondria-localized heterodimeric transglycosylase","volume":"284","author":"Boland","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2026081413085818800_cit18","doi-asserted-by":"publisher","first-page":"958","DOI":"10.1261\/rna.1997610","article-title":"Characterization\nof the human tRNA-guanine transglycosylase: confirmation of the heterodimeric\nsubunit structure","volume":"16","author":"Chen","year":"2010","journal-title":"RNA"},{"key":"2026081413085818800_cit19","doi-asserted-by":"publisher","first-page":"3953","DOI":"10.1021\/acs.biochem.8b00294","article-title":"Homodimer architecture of QTRT2, the noncatalytic subunit\nof the eukaryotic tRNA-guanine transglycosylase","volume":"57","author":"Behrens","year":"2018","journal-title":"Biochemistry"},{"key":"2026081413085818800_cit20","doi-asserted-by":"publisher","first-page":"81","DOI":"10.3390\/biom8030081","article-title":"Crystal structure\nof the human tRNA\nguanine transglycosylase catalytic subunit QTRT1","volume":"8","author":"Johannsson","year":"2018","journal-title":"Biomolecules"},{"key":"2026081413085818800_cit21","doi-asserted-by":"publisher","first-page":"4627","DOI":"10.1128\/jb.176.15.4627-4634.1994","article-title":"vacC, a virulence-associated\nchromosomal\nlocus of Shigella flexneri, is homologous to tgt,\na gene encoding tRNA-guanine transglycosylase (Tgt) of Escherichia\ncoli K-12","volume":"176","author":"Durand","year":"1994","journal-title":"J. Bacteriol."},{"key":"2026081413085818800_cit22","doi-asserted-by":"publisher","first-page":"19354","DOI":"10.1074\/jbc.m111.219576","article-title":"Queuosine deficiency\nin eukaryotes comprises tyrosine\nproduction through increased tetrahydrobiopterin oxidation","volume":"286","author":"Rakovich","year":"2011","journal-title":"J. Biol. Chem."},{"key":"2026081413085818800_cit23","doi-asserted-by":"publisher","first-page":"2029","DOI":"10.1093\/nar\/gkw847","article-title":"In vivo\nmodification of tRNA with an artificial nucleobase leads to full disease\nremission in an animal model of multiple sclerosis","volume":"45","author":"Varghese","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"2026081413085818800_cit24","doi-asserted-by":"publisher","DOI":"10.3390\/cancers12030628","article-title":"tRNA queuosine modification enzyme modulates the growth\nand microbiome recruitment to breast tumors","volume":"12","author":"Zhang","year":"2020","journal-title":"Cancers"},{"key":"2026081413085818800_cit25","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.03549-20","article-title":"Queuine is a nutritional regulator of\nEntamoeba histolytica response to oxidative stress and a virulence\nattenuator","volume":"12","author":"Nagaraja","year":"2021","journal-title":"mBio"},{"key":"2026081413085818800_cit26","doi-asserted-by":"publisher","first-page":"8247","DOI":"10.1093\/nar\/gkab567","article-title":"Preferential import\nof queuosine-modified tRNAs into Tryposoma brucei mitochondrion is\ncritical for organellar protein synthesis","volume":"49","author":"Kulkarni","year":"2021","journal-title":"Nucleic\nAcids Res."},{"key":"2026081413085818800_cit27","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0175723","article-title":"Soaking suggests \u201calternative\nfacts\u201d: only cocrystallization discloses major ligand-induced\ninterface rearrangements of a homodimeric tRNA-binding protein indicating\na novel mode-of-inhibition","volume":"12","author":"Ehrmann","year":"2017","journal-title":"PLoS One"},{"key":"2026081413085818800_cit28","doi-asserted-by":"publisher","first-page":"10085","DOI":"10.1002\/anie.201804627","article-title":"Swapping interface contacts\nin the homodimeric tRNA-guanine transglycosylase: an option for functional\nregulation","volume":"57","author":"Ehrmann","year":"2018","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026081413085818800_cit29","doi-asserted-by":"publisher","first-page":"23419","DOI":"10.1002\/anie.202108179","article-title":"Unraveling a ligand-induced twist\nof a homodimeric enzyme by pulsed-electron-electron double resonance","volume":"60","author":"Nguyen","year":"2021","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026081413085818800_cit30","doi-asserted-by":"publisher","first-page":"2713","DOI":"10.1002\/prot.24637","article-title":"Hot-spot analysis to dissect the\nfunctional protein-protein interface of a tRNA-modifying enzyme","volume":"82","author":"Jakobi","year":"2014","journal-title":"Proteins: Struct., Funct., Bioinf."},{"key":"2026081413085818800_cit31","doi-asserted-by":"publisher","first-page":"1441","DOI":"10.1021\/acs.accounts.7b00109","article-title":"Ten good reasons for the use of the tellurium-centered\nAnderson-Evans polyoxotungstate in protein crystallography","volume":"50","author":"Bijelic","year":"2017","journal-title":"Acc. Chem. Res."},{"key":"2026081413085818800_cit32","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1016\/j.molstruc.2006.04.027","article-title":"First Strandberg-type\npolyoxotungstate compound: Synthesis and characterization of organic-inorganic\nhybrid (H2en)\u00ad(Hen)2[H2P2W5O23]\u00b75.42H2O","volume":"825","author":"Lin","year":"2006","journal-title":"J. Mol. Struct."},{"key":"2026081413085818800_cit33","doi-asserted-by":"publisher","first-page":"1897","DOI":"10.1021\/acschembio.5b00028","article-title":"What glues a homodimer\ntogether:\nsystematic analysis of the stabilizing effect of an aromatic hot spot\nin the protein-protein interface of the tRNA-modifying enzyme Tgt","volume":"10","author":"Jakobi","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"2026081413085818800_cit34","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1080\/15476286.2021.1950980","article-title":"Structural and functional\ninsights into human tRNA-guanine transglycosylase","volume":"18","author":"Sievers","year":"2021","journal-title":"RNA Biol."},{"key":"2026081413085818800_cit35","doi-asserted-by":"publisher","first-page":"3021","DOI":"10.1021\/acschembio.0c00700","article-title":"The importance of charge\nin perturbing the aromatic glue stabilizing the protein-protein interface\nof homodimeric tRNA-guanine transglycosylase","volume":"15","author":"Nguyen","year":"2020","journal-title":"ACS Chem. Biol."},{"key":"2026081413085818800_cit36","doi-asserted-by":"publisher","first-page":"15381","DOI":"10.1021\/bi00046a047","article-title":"tRNA-guanine\ntransglycosylase from\nEscherichia coli: structure-activity studies investigating the role\nof the aminomethyl substituent of the heterocyclic substrate preQ1","volume":"34","author":"Hoops","year":"1995","journal-title":"Biochemistry"},{"key":"2026081413085818800_cit37","doi-asserted-by":"publisher","first-page":"3067","DOI":"10.1016\/s0021-9258(17)30183-7","article-title":"Novel mechanism\nof post-transcriptional modification of tRNA. Insertion of bases of\nQ precursors into tRNA by a specific tRNA transglycosylase reaction","volume":"254","author":"Okada","year":"1979","journal-title":"J. Biol. Chem."},{"key":"2026081413085818800_cit38","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1016\/0167-4781(84)90124-6","article-title":"Substrate and inhibitor specificity\nof tRNA-guanine ribosyltransferase","volume":"781","author":"Farkas","year":"1984","journal-title":"Biochim.\nBiophys. Acta"},{"key":"2026081413085818800_cit39","doi-asserted-by":"publisher","first-page":"764","DOI":"10.1016\/j.jmb.2007.09.062","article-title":"Glutamate versus glutamine\nexchange swaps substrate\nselectivity in tRNA-guanine transglycosylase: Insight into the regulation\nof substrate selectivity by kinetic and crystallographic studies","volume":"374","author":"Tidten","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2026081413085818800_cit40","doi-asserted-by":"publisher","first-page":"1066","DOI":"10.1002\/cbic.200300644","article-title":"Flexible adaptations\nin the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase\nand their implications for substrate selectivity, reaction mechanism\nand structure-based drug design","volume":"4","author":"Brenk","year":"2003","journal-title":"ChemBioChem"},{"key":"2026081413085818800_cit41","doi-asserted-by":"publisher","first-page":"2834","DOI":"10.1093\/nar\/gkq1188","article-title":"Evolution of eukaryal tRNA-guanine\ntransglycosylase: insight gained from the heterocyclic substrate recognition\nby the wild-type and mutant human and Escherichia coli tRNA-guanine\ntransglycosylases","volume":"39","author":"Chen","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"2026081413085818800_cit42","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0064240","article-title":"Investigation\nof specificity determinants in bacterial tRNA-guanine transglycosylase\nreveals queuine, the substrate of its eucaryotic counterpart, as inhibitor","volume":"8","author":"Biela","year":"2013","journal-title":"PLoS One"},{"key":"2026081413085818800_cit43","doi-asserted-by":"publisher","first-page":"3915","DOI":"10.1039\/c9cc09887a","article-title":"The eukaryotic\ntRNA-guanine transglycosylase enzyme inserts queuine via a sequential\nbi-bi mechanism","volume":"56","author":"Alqasem","year":"2020","journal-title":"Chem. Commun."},{"key":"2026081413085818800_cit44","doi-asserted-by":"publisher","first-page":"4877","DOI":"10.1093\/nar\/gkab289","article-title":"The human tRNA-guanine\ntransglycosylase displays promiscuous nucleobase preference but strict\ntRNA specificity","volume":"49","author":"Fergus","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"2026081413085818800_cit45","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1006\/jmbi.2000.4256","article-title":"A new target\nfor shigellosis: rational design and crystallographic studies of inhibitors\nof tRNA-guanine transglycosylase","volume":"306","author":"Gra\u0308dler","year":"2001","journal-title":"J. Mol. Biol."},{"key":"2026081413085818800_cit46","doi-asserted-by":"publisher","first-page":"5239","DOI":"10.1021\/bi00070a036","article-title":"tRNA-guanine\ntransglycosylase\nfrom Escherichia coli: gross tRNA structural requirements for recognition","volume":"32","author":"Curnow","year":"1993","journal-title":"Biochemistry"},{"key":"2026081413085818800_cit47","doi-asserted-by":"publisher","first-page":"8660","DOI":"10.1039\/c2ob26387d","article-title":"Concise and efficient\nsyntheses of preQ1 base, Q base\nand (ent)-Q base","volume":"10","author":"Gerber","year":"2012","journal-title":"Org. Biomol.\nChem."},{"key":"2026081413085818800_cit48","doi-asserted-by":"publisher","first-page":"3317","DOI":"10.1080\/00397919608004641","article-title":"A two step synthesis\nof the nucleoside Q precursor 2-amino-5-cyanopyrrolo\u00ad[2,3-d]\u00adpyrimidin-4-one (preQ0)","volume":"26","author":"Migawa","year":"1996","journal-title":"Synth.\nCommun."},{"key":"2026081413085818800_cit49","doi-asserted-by":"publisher","first-page":"1085","DOI":"10.1107\/s1600576716004416","article-title":"XDSAPP2.0","volume":"49","author":"Sparta","year":"2016","journal-title":"J. Appl. Crystallogr."},{"key":"2026081413085818800_cit50","doi-asserted-by":"publisher","first-page":"582","DOI":"10.1107\/s0907444909012098","article-title":"Decision-making\nin structure solution using Bayesian estimates of map quality: the\nPHENIX AutoSol wizard","volume":"65","author":"Terwilliger","year":"2009","journal-title":"Acta Crystallogr., Sect.\nD: Struct. 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