{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T13:51:12Z","timestamp":1790862672263,"version":"4.1.0"},"reference-count":38,"publisher":"National Academy of Sciences","issue":"9","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2012,2,28]]},"abstract":"<jats:p>\n                    Aminoacyl-tRNA synthetases (aaRSs) ensure faithful translation of mRNA into protein by coupling an amino acid to a set of tRNAs with conserved anticodon sequences. Here, we show that in mitochondria of\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    , a single aaRS (MST1) recognizes and aminoacylates two natural tRNAs that contain anticodon loops of different size and sequence. Besides a regular\n                    <jats:inline-formula>\n                      <jats:inline-graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"pnas.1200109109eq1.gif\"\/>\n                    <\/jats:inline-formula>\n                    with a threonine (Thr) anticodon, MST1 also recognizes an unusual\n                    <jats:inline-formula>\n                      <jats:inline-graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"pnas.1200109109eq2.gif\"\/>\n                    <\/jats:inline-formula>\n                    , which contains an enlarged anticodon loop and an anticodon triplet that reassigns the CUN codons from leucine to threonine. Our data show that MST1 recognizes the anticodon loop in both tRNAs, but employs distinct recognition mechanisms. The size but not the sequence of the anticodon loop is critical for\n                    <jats:inline-formula>\n                      <jats:inline-graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"pnas.1200109109eq3.gif\"\/>\n                    <\/jats:inline-formula>\n                    recognition, whereas the anticodon sequence is essential for aminoacylation of\n                    <jats:inline-formula>\n                      <jats:inline-graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"pnas.1200109109eq4.gif\"\/>\n                    <\/jats:inline-formula>\n                    . The crystal structure of MST1 reveals that, while lacking the N-terminal editing domain, the enzyme closely resembles the bacterial threonyl-tRNA synthetase (ThrRS). A detailed structural comparison with\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    ThrRS, which is unable to aminoacylate\n                    <jats:inline-formula>\n                      <jats:inline-graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"pnas.1200109109eq5.gif\"\/>\n                    <\/jats:inline-formula>\n                    , reveals differences in the anticodon-binding domain that probably allow recognition of the distinct anticodon loops. Finally, our mutational and modeling analyses identify the structural elements in MST1 (e.g., helix \u03b111) that define tRNA selectivity. Thus, MTS1 exemplifies that a single aaRS can recognize completely divergent anticodon loops of natural isoacceptor tRNAs and that in doing so it facilitates the reassignment of the genetic code in yeast mitochondria.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1200109109","type":"journal-article","created":{"date-parts":[[2012,2,18]],"date-time":"2012-02-18T00:29:26Z","timestamp":1329524966000},"page":"3281-3286","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":30,"title":["Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment"],"prefix":"10.1073","volume":"109","author":[{"given":"Jiqiang","family":"Ling","sequence":"first","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaitlyn M.","family":"Peterson","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivana","family":"Simonovi\u0107","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chris","family":"Cho","sequence":"additional","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dieter","family":"S\u00f6ll","sequence":"additional","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;"},{"name":"Department of Chemistry, Yale University, New Haven, CT 06520"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miljan","family":"Simonovi\u0107","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2012,2,17]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1146\/annurev.biochem.69.1.617","article-title":"Aminoacyl-tRNA synthesis","volume":"69","author":"Ibba M","year":"2000","unstructured":"M Ibba, D S\u00f6ll, Aminoacyl-tRNA synthesis. Annu Rev Biochem 69, 617\u2013650 (2000).","journal-title":"Annu Rev Biochem"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1038\/nrm2352","article-title":"A structural understanding of the dynamic ribosome machine","volume":"9","author":"Steitz TA","year":"2008","unstructured":"TA Steitz, A structural understanding of the dynamic ribosome machine. Nat Rev Mol Cell Biol 9, 242\u2013253 (2008).","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"3342","DOI":"10.1021\/bi00660a026","article-title":"Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing","volume":"15","author":"Fersht AR","year":"1976","unstructured":"AR Fersht, MM Kaethner, Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing. Biochemistry 15, 3342\u20133346 (1976).","journal-title":"Biochemistry"},{"key":"e_1_3_4_4_2","first-page":"153","volume-title":"Protein Engineering","author":"Mascarenhas AP","year":"2008","unstructured":"AP Mascarenhas, S An, AE Rosen, SA Martinis, K Musier-Forsyth, Fidelity Mechanisms of the Aminoacyl-tRNA Synthetases. Protein Engineering, eds UL RajBhandary, C K\u00f6hrer (Springer-Verlag, New York), pp. 153\u2013200 (2008)."},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1146\/annurev.micro.091208.073210","article-title":"Aminoacyl-tRNA synthesis and translational quality control","volume":"63","author":"Ling J","year":"2009","unstructured":"J Ling, N Reynolds, M Ibba, Aminoacyl-tRNA synthesis and translational quality control. Annu Rev Microbiol 63, 61\u201378 (2009).","journal-title":"Annu Rev Microbiol"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"15422","DOI":"10.1073\/pnas.2136934100","article-title":"Trans-editing of mischarged tRNAs","volume":"100","author":"Ahel I","year":"2003","unstructured":"I Ahel, D Korencic, M Ibba, D S\u00f6ll, Trans-editing of mischarged tRNAs. Proc Natl Acad Sci USA 100, 15422\u201315427 (2003).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"42359","DOI":"10.1074\/jbc.C400304200","article-title":"Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK protein","volume":"279","author":"An S","year":"2004","unstructured":"S An, K Musier-Forsyth, Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK protein. J Biol Chem 279, 42359\u201342362 (2004).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"30073","DOI":"10.1074\/jbc.M805943200","article-title":"Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation","volume":"283","author":"Chong YE","year":"2008","unstructured":"YE Chong, XL Yang, P Schimmel, Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. J Biol Chem 283, 30073\u201330078 (2008).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"5017","DOI":"10.1093\/nar\/26.22.5017","article-title":"Universal rules and idiosyncratic features in tRNA identity","volume":"26","author":"Gieg\u00e9 R","year":"1998","unstructured":"R Gieg\u00e9, M Sissler, C Florentz, Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res 26, 5017\u20135035 (1998).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/j.molcel.2007.01.015","article-title":"Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase","volume":"25","author":"Guth EC","year":"2007","unstructured":"EC Guth, CS Francklyn, Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase. Mol Cell 25, 531\u2013542 (2007).","journal-title":"Mol Cell"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"6800","DOI":"10.1021\/bi00443a003","article-title":"Evidence that a major determinant for the identity of a transfer RNA is conserved in evolution","volume":"28","author":"Hou YM","year":"1989","unstructured":"YM Hou, P Schimmel, Evidence that a major determinant for the identity of a transfer RNA is conserved in evolution. Biochemistry 28, 6800\u20136804 (1989).","journal-title":"Biochemistry"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1126\/science.8128220","article-title":"The 2.9\u00a0A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA","volume":"263","author":"Biou V","year":"1994","unstructured":"V Biou, A Yaremchuk, M Tukalo, S Cusack, The 2.9\u00a0A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA. Science 263, 1404\u20131410 (1994).","journal-title":"Science"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/0092-8674(79)90352-0","article-title":"Assembly of the mitochondrial membrane system: Sequences of yeast mitochondrial valine and an unusual threonine tRNA gene","volume":"18","author":"Li M","year":"1979","unstructured":"M Li, A Tzagoloff, Assembly of the mitochondrial membrane system: Sequences of yeast mitochondrial valine and an unusual threonine tRNA gene. Cell 18, 47\u201353 (1979).","journal-title":"Cell"},{"key":"e_1_3_4_14_2","first-page":"205","article-title":"Similarities and differences in tRNA identity between Escherichia coli and Saccharomyces cerevisiae: Evolutionary conservation and divergence","volume":"34","author":"Nameki N","year":"1995","unstructured":"N Nameki, et al., Similarities and differences in tRNA identity between Escherichia coli and Saccharomyces cerevisiae: Evolutionary conservation and divergence. Nucleic Acids Symp Ser 34, 205\u2013206 (1995).","journal-title":"Nucleic Acids Symp Ser"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/0014-5793(96)01094-0","article-title":"Identity elements of Thermus thermophilus tRNAThr","volume":"396","author":"Nameki N","year":"1996","unstructured":"N Nameki, H Asahara, T Hasegawa, Identity elements of Thermus thermophilus tRNAThr. FEBS Lett 396, 201\u2013207 (1996).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/S0092-8674(00)80746-1","article-title":"The structure of threonyl-tRNA synthetase-tRNAThr complex enlightens its repressor activity and reveals an essential zinc ion in the active site","volume":"97","author":"Sankaranarayanan R","year":"1999","unstructured":"R Sankaranarayanan, et al., The structure of threonyl-tRNA synthetase-tRNAThr complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97, 371\u2013381 (1999).","journal-title":"Cell"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"4866","DOI":"10.1093\/nar\/gkr073","article-title":"An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine","volume":"39","author":"Su D","year":"2011","unstructured":"D Su, et al., An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine. Nucleic Acids Res 39, 4866\u20134874 (2011).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"5069","DOI":"10.1002\/j.1460-2075.1996.tb00887.x","article-title":"Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts","volume":"15","author":"Sissler M","year":"1996","unstructured":"M Sissler, R Gieg\u00e9, C Florentz, Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts. EMBO J 15, 5069\u20135076 (1996).","journal-title":"EMBO J"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1038\/nsb0994-580","article-title":"A single methyl group prevents the mischarging of a tRNA","volume":"1","author":"Putz J","year":"1994","unstructured":"J Putz, C Florentz, F Benseler, R Gieg\u00e9, A single methyl group prevents the mischarging of a tRNA. Nat Struct Biol 1, 580\u2013582 (1994).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"4936","DOI":"10.1073\/pnas.80.16.4936","article-title":"Anticodon shift in tRNA: A novel mechanism in missense and nonsense suppression","volume":"80","author":"Murgola EJ","year":"1983","unstructured":"EJ Murgola, NE Prather, BH Mims, FT Pagel, KA Hijazi, Anticodon shift in tRNA: A novel mechanism in missense and nonsense suppression. Proc Natl Acad Sci USA 80, 4936\u20134939 (1983).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"7408","DOI":"10.1073\/pnas.78.12.7408","article-title":"Nucleotide insertion in the anticodon loop of a glycine transfer RNA causes missense suppression","volume":"78","author":"Prather NE","year":"1981","unstructured":"NE Prather, EJ Murgola, BH Mims, Nucleotide insertion in the anticodon loop of a glycine transfer RNA causes missense suppression. Proc Natl Acad Sci USA 78, 7408\u20137411 (1981).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"46770","DOI":"10.1074\/jbc.M105150200","article-title":"Dual mode recognition of two isoacceptor tRNAs by mammalian mitochondrial seryl-tRNA synthetase","volume":"276","author":"Shimada N","year":"2001","unstructured":"N Shimada, T Suzuki, K Watanabe, Dual mode recognition of two isoacceptor tRNAs by mammalian mitochondrial seryl-tRNA synthetase. J Biol Chem 276, 46770\u201346778 (2001).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"3369","DOI":"10.1038\/sj.emboj.7600811","article-title":"Dual-mode recognition of noncanonical tRNAsSer by seryl-tRNA synthetase in mammalian mitochondria","volume":"24","author":"Chimnaronk S","year":"2005","unstructured":"S Chimnaronk, M Gravers Jeppesen, T Suzuki, J Nyborg, K Watanabe, Dual-mode recognition of noncanonical tRNAsSer by seryl-tRNA synthetase in mammalian mitochondria. EMBO J 24, 3369\u20133379 (2005).","journal-title":"EMBO J"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S1097-2765(04)00591-X","article-title":"Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution","volume":"16","author":"Dock-Bregeon AC","year":"2004","unstructured":"AC Dock-Bregeon, et al., Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution. Mol Cell 16, 375\u2013386 (2004).","journal-title":"Mol Cell"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"5958","DOI":"10.1073\/pnas.0401530101","article-title":"A domain for editing by an archaebacterial tRNA synthetase","volume":"101","author":"Beebe K","year":"2004","unstructured":"K Beebe, E Merriman, L Ribas De Pouplana, P Schimmel, A domain for editing by an archaebacterial tRNA synthetase. Proc Natl Acad Sci USA 101, 5958\u20135963 (2004).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"4152","DOI":"10.1038\/sj.emboj.7601278","article-title":"Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea","volume":"25","author":"Hussain T","year":"2006","unstructured":"T Hussain, et al., Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea. EMBO J 25, 4152\u20134162 (2006).","journal-title":"EMBO J"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"10260","DOI":"10.1073\/pnas.0403926101","article-title":"A freestanding proofreading domain is required for protein synthesis quality control in Archaea","volume":"101","author":"Korencic D","year":"2004","unstructured":"D Korencic, et al., A freestanding proofreading domain is required for protein synthesis quality control in Archaea. Proc Natl Acad Sci USA 101, 10260\u201310265 (2004).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"9378","DOI":"10.1073\/pnas.1016460108","article-title":"Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites","volume":"108","author":"Li L","year":"2011","unstructured":"L Li, et al., Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites. Proc Natl Acad Sci USA 108, 9378\u201383 (2011).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/75856","article-title":"Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase","volume":"7","author":"Sankaranarayanan R","year":"2000","unstructured":"R Sankaranarayanan, et al., Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase. Nat Struct Biol 7, 461\u2013465 (2000).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"38186","DOI":"10.1074\/jbc.M508281200","article-title":"Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase","volume":"280","author":"Roy H","year":"2005","unstructured":"H Roy, J Ling, J Alfonzo, M Ibba, Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase. J Biol Chem 280, 38186\u201338192 (2005).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"4063","DOI":"10.1073\/pnas.0909640107","article-title":"Cell-specific differences in the requirements for translation quality control","volume":"107","author":"Reynolds NM","year":"2010","unstructured":"NM Reynolds, et al., Cell-specific differences in the requirements for translation quality control. Proc Natl Acad Sci USA 107, 4063\u20134068 (2010).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"23810","DOI":"10.1074\/jbc.M110.105320","article-title":"Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase","volume":"285","author":"Minajigi A","year":"2010","unstructured":"A Minajigi, CS Francklyn, Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase. J Biol Chem 285, 23810\u201323817 (2010).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"4028","DOI":"10.1073\/pnas.1000315107","article-title":"Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site","volume":"107","author":"Ling J","year":"2010","unstructured":"J Ling, D S\u00f6ll, Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site. Proc Natl Acad Sci USA 107, 4028\u20134033 (2010).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"16502","DOI":"10.1073\/pnas.0809179105","article-title":"Quality control despite mistranslation caused by an ambiguous genetic code","volume":"105","author":"Ruan B","year":"2008","unstructured":"B Ruan, et al., Quality control despite mistranslation caused by an ambiguous genetic code. Proc Natl Acad Sci USA 105, 16502\u201316507 (2008).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1038\/nrmicro2472","article-title":"Cellular mechanisms that control mistranslation","volume":"8","author":"Reynolds NM","year":"2010","unstructured":"NM Reynolds, BA Lazazzera, M Ibba, Cellular mechanisms that control mistranslation. Nat Rev Microbiol 8, 849\u2013856 (2010).","journal-title":"Nat Rev Microbiol"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1038\/nature08576","article-title":"Innate immune and chemically triggered oxidative stress modifies translational fidelity","volume":"462","author":"Netzer N","year":"2009","unstructured":"N Netzer, et al., Innate immune and chemically triggered oxidative stress modifies translational fidelity. Nature 462, 522\u2013526 (2009).","journal-title":"Nature"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1073\/pnas.85.4.1033","article-title":"Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro","volume":"85","author":"Sampson JR","year":"1988","unstructured":"JR Sampson, OC Uhlenbeck, Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc Natl Acad Sci USA 85, 1033\u20131037 (1988).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"4639","DOI":"10.1038\/sj.emboj.7600474","article-title":"Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase","volume":"23","author":"Roy H","year":"2004","unstructured":"H Roy, J Ling, M Irnov, M Ibba, Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. EMBO J 23, 4639\u20134648 (2004).","journal-title":"EMBO J"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1200109109","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T05:39:18Z","timestamp":1654580358000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1200109109"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,2,17]]},"references-count":38,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2012,2,28]]}},"alternative-id":["10.1073\/pnas.1200109109"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1200109109","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,2,17]]},"assertion":[{"value":"2012-02-17","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}