The modified base isopentenyladenosine and its derivatives in tRNA

References

• Bjork GR, Ericson JU, Gustafsson CE, Hagervall TG, Jonsson YH, Wikstrom PM. Transfer RNA modification. Annu Rev Biochem 1987; 56:263-87; PMID:3304135; http://dx.doi.org/10.1146/annurev.bi.56.070187.001403
   PubMed Web of Science ®Google Scholar
• El Yacoubi B, Bailly M, de Crecy-Lagard V. Biosynthesis and function of posttranscriptional modifications of transfer RNAs. Annu Rev Genet 2012; 46:69-95; PMID:22905870; http://dx.doi.org/10.1146/annurev-genet-110711-155641
   PubMed Web of Science ®Google Scholar
• Persson BC, Esberg B, Olafsson O, Bjork GR. Synthesis and function of isopentenyl adenosine derivatives in tRNA. Biochimie 1994; 76:1152-60; PMID:7748950; http://dx.doi.org/10.1016/0300-9084(94)90044-2
   PubMed Web of Science ®Google Scholar
• Soll D. Enzymatic modification of transfer RNA. Science 1971; 173:293-9; PMID:4934576; http://dx.doi.org/10.1126/science.173.3994.293
   PubMed Web of Science ®Google Scholar
• Grosjean H, Westhof E. An integrated, structure- and energy-based view of the genetic code. Nucleic Acids Res 2016; 44:8020-40; PMID:27448410; http://dx.doi.org/10.1093/nar/gkw608
   PubMed Web of Science ®Google Scholar
• Murphy FV, Ramakrishnan V, Malkiewicz A, Agris PF. The role of modifications in codon discrimination by tRNA(Lys) UUU. Nat Struct Mol Biol 2004; 11:1186-91; http://dx.doi.org/10.1038/nsmb861
   PubMed Web of Science ®Google Scholar
• Weixlbaumer AM,   F. V. IV. Crystallographic Studies of Decoding by Modified Bases: Correlation of Structure and Function. In: Grosjean H, ed. DNA and RNA Modification Enzymes: Structure, Mechanism, Function and Evolution: Landes Bioscience, 2009:493-508
   Google Scholar
• Suzuki T, Suzuki T. A complete landscape of post-transcriptional modifications in mammalian mitochondrial tRNAs. Nucleic Acids Res 2014; 42:7346-57; PMID:24831542; http://dx.doi.org/10.1093/nar/gku390
   PubMed Web of Science ®Google Scholar
• Deutsch C, El Yacoubi B, de Crecy-Lagard V, Iwata-Reuyl D. Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside. J Biol Chem 2012; 287:13666-73; PMID:22378793; http://dx.doi.org/10.1074/jbc.M112.344028
   PubMed Web of Science ®Google Scholar
• Perche-Letuvee P, Molle T, Forouhar F, Mulliez E, Atta M. Wybutosine biosynthesis: structural and mechanistic overview. RNA Biol 2014; 11:1508-18; PMID:25629788; http://dx.doi.org/10.4161/15476286.2014.992271
   PubMed Web of Science ®Google Scholar
• Lamichhane TN, Mattijssen S, Maraia RJ. Human cells have a limited set of tRNA anticodon loop substrates of the tRNA isopentenyltransferase TRIT1 tumor suppressor. Mol Cell Biol 2013; 33:4900-8; PMID:24126054; http://dx.doi.org/10.1128/MCB.01041-13
   PubMed Web of Science ®Google Scholar
• Motorin Y, Bec G, Tewari R, Grosjean H. Transfer RNA recognition by the Escherichia coli Delta(2)-isopentenyl-pyrophosphate:tRNA Delta 2-isopentenyl transferase: Dependence on the anticodon arm structure. RNA 1997; 3:721-33; PMID:9214656
   PubMed Web of Science ®Google Scholar
• Juhling F, Morl M, Hartmann RK, Sprinzl M, Stadler PF, Putz J. tRNAdb 2009: compilation of tRNA sequences and tRNA genes. Nucleic Acids Res 2009; 37:D159-62; PMID:18957446; http://dx.doi.org/10.1093/nar/gkn772
   PubMed Web of Science ®Google Scholar
• Dunin-Horkawicz S, Czerwoniec A, Gajda MJ, Feder M, Grosjean H, Bujnicki JM. MODOMICS: a database of RNA modification pathways. Nucleic Acids Res 2006; 34:D145-9; PMID:16381833; http://dx.doi.org/10.1093/nar/gkj084
   PubMed Web of Science ®Google Scholar
• Machnicka MA, Milanowska K, Osman Oglou O, Purta E, Kurkowska M, Olchowik A, Olchowik A, Januszewski W, Kalinowski S, Dunin-Horkawicz S, et al. MODOMICS: a database of RNA modification pathways–2013 update. Nucleic Acids Res 2013; 41:D262-7; PMID:23118484; http://dx.doi.org/10.1093/nar/gks1007
   PubMed Web of Science ®Google Scholar
• Zachau HG, Dutting D, Feldmann H. Nucleotide sequences of two serine-specific transfer ribonucleic acids. Angew Chem Int Ed Engl 1966; 5:422; PMID:4956644; http://dx.doi.org/10.1002/anie.196604221
   PubMed Web of Science ®Google Scholar
• Hall RH, Robins MJ, Stasiuk L, Thedford R. Isolation of N6-(Gamma Gamma-Dimethylallyl)Adenosine from Soluble Ribonucleic Acid. JACS 1966; 88:2614; http://dx.doi.org/10.1021/ja00963a061
   Web of Science ®Google Scholar
• Bartz J, Soll D, Burrows WJ, Skoog F. Identification of Cytokinin-Active Ribonucleosides in Pure Escherichia-Coli Transfer Rna Species. P Natl Acad Sci USA 1970; 67:1448; PMID:4922291; http://dx.doi.org/10.1073/pnas.67.3.1448
   PubMed Web of Science ®Google Scholar
• Bartz JK, Kline LK, Soll D. N6-(Delta2-Isopentenyl)Adenosine - Biosynthesis in-Vitro in Transfer Rna by an Enzyme Purified from Escherichia-Coli. Biochem Bioph Res Co 1970; 40:1481; PMID:4326583; http://dx.doi.org/10.1016/0006-291X(70)90035-5
   PubMed Web of Science ®Google Scholar
• Agris PF, Armstrong DJ, Schafer KP, Soll D. Maturation of a Hypermodified Nucleoside in Transfer-Rna. Nucleic Acids Res 1975; 2:691-8; PMID:49880; http://dx.doi.org/10.1093/nar/2.5.691
   PubMed Web of Science ®Google Scholar
• Caillet J, Droogmans L. Molecular-Cloning of the Escherichia-Coli Miaa Gene Involved in the Formation of Delta-2-Isopentenyl Adenosine in Transfer-Rna. J Bacteriol 1988; 170:4147-52; PMID:3045085; http://dx.doi.org/10.1128/jb.170.9.4147-4152.1988
   PubMed Web of Science ®Google Scholar
• Eisenberg SP, Yarus M, Soll L. The effect of an Escherichia coli regulatory mutation on transfer RNA structure. J Mol Biol 1979; 135:111-26; PMID:93644; http://dx.doi.org/10.1016/0022-2836(79)90343-7
   PubMed Web of Science ®Google Scholar
• Landgraf BJ, McCarthy EL, Booker SJ. Radical S-Adenosylmethionine Enzymes in Human Health and Disease. Annu Rev Biochem 2016; 85:485-514; PMID:27145839; http://dx.doi.org/10.1146/annurev-biochem-060713-035504
   PubMed Web of Science ®Google Scholar
• Laten H, Gorman J, Bock RM. Isopentenyladenosine deficient tRNA from an antisuppressor mutant of Saccharomyces cerevisiae. Nucleic Acids Res 1978; 5:4329-42; PMID:364426; http://dx.doi.org/10.1093/nar/5.11.4329
   PubMed Web of Science ®Google Scholar
• Dihanich ME, Najarian D, Clark R, Gillman EC, Martin NC, Hopper AK. Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae. Mol Cell Biol 1987; 7:177-84; PMID:3031456; http://dx.doi.org/10.1128/MCB.7.1.177
   PubMed Web of Science ®Google Scholar
• Connolly DM, Winkler ME. Genetic and physiological relationships among the miaA gene, 2-methylthio-N6-(delta 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12. J Bacteriol 1989; 171:3233-46; PMID:2656644; http://dx.doi.org/10.1128/jb.171.6.3233-3246.1989
   PubMed Web of Science ®Google Scholar
• Golovko A, Hjalm G, Sitbon F, Nicander B. Cloning of a human tRNA isopentenyl transferase. Gene 2000; 258:85-93; PMID:11111046; http://dx.doi.org/10.1016/S0378-1119(00)00421-2
   PubMed Web of Science ®Google Scholar
• Reiter V, Matschkal DM, Wagner M, Globisch D, Kneuttinger AC, Muller M, Carell T. The CDK5 repressor CDK5RAP1 is a methylthiotransferase acting on nuclear and mitochondrial RNA. Nucleic Acids Res 2012; 40:6235-40; PMID:22422838; http://dx.doi.org/10.1093/nar/gks240
   PubMed Web of Science ®Google Scholar
• Arragain S, Handelman SK, Forouhar F, Wei FY, Tomizawa K, Hunt JF, Douki T, Fontecave M, Mulliez E, Atta M. Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA. J Biol Chem 2010; 285:28425-33; PMID:20584901; http://dx.doi.org/10.1074/jbc.M110.106831
   PubMed Web of Science ®Google Scholar
• Armstrong DJ, Burrows WJ, Skoog F, Roy KL, Soll D. Cytokinins - Distribution in Transfer Rna Species of Escherichia Coli. Proc Natl Acad Sci USA 1969; 63:834; PMID:4899879; http://dx.doi.org/10.1073/pnas.63.3.834
   PubMed Web of Science ®Google Scholar
• Schön A, Böck A, Ott G, Sprinzl M, Söll D. The selenocysteine-inserting opal suppressor serine tRNA from E. coli is highly unusual in structure and modification. Nucleic Acids Res 1989; 17:7159-65; PMID:2529478; http://dx.doi.org/10.1093/nar/17.18.7159
   PubMed Web of Science ®Google Scholar
• Gefter ML, Russell RL. Role of Modifications in Tyrosine Transfer Rna - a Modified Base Affecting Ribosome Binding. J Mol Biol 1969; 39:145; PMID:4938812; http://dx.doi.org/10.1016/0022-2836(69)90339-8
   PubMed Web of Science ®Google Scholar
• Buck M, Griffiths E. Iron Mediated Methylthiolation of Transfer-Rna as a Regulator of Operon Expression in Escherichia-Coli. Nucleic Acids Res 1982; 10:2609-24; PMID:7043398; http://dx.doi.org/10.1093/nar/10.8.2609
   PubMed Web of Science ®Google Scholar
• Mclennan BD, Buck M, Humphreys J, Griffiths E. Iron-Related Modification of Bacterial Transfer-Rna. Nucleic Acids Res 1981; 9:2629-40; PMID:6792594; http://dx.doi.org/10.1093/nar/9.11.2629
   PubMed Web of Science ®Google Scholar
• Buck M, Griffiths E. Regulation of Aromatic Amino-Acid-Transport by Transfer-Rna - Role of 2-Methylthio-N6-(Delta-2-Isopentenyl)-Adenosine. Nucleic Acids Res 1981; 9:401-14; PMID:7010315; http://dx.doi.org/10.1093/nar/9.2.401
   PubMed Web of Science ®Google Scholar
• Griffiths E, Humphreys J. Alterations in Transfer-Rnas Containing 2-Methylthio-N6-(Delta-2-Isopentenyl)-Adenosine during Growth of Enteropathogenic Escherichia-Coli in Presence of Iron-Binding Proteins. Euro J Biochem 1978; 82:503-13; PMID:342239; http://dx.doi.org/10.1111/j.1432-1033.1978.tb12044.x
   PubMedGoogle Scholar
• Buck M, Ames BN. A modified nucleotide in Transfer-Rna as a possible regulator of aerobiosis - synthesis of Cis-2-methylthioribosylzeatin in the transfer-Rna of salmonella. Cell 1984; 36:523-31; PMID:6362893; http://dx.doi.org/10.1016/0092-8674(84)90245-9
   PubMed Web of Science ®Google Scholar
• Diaz I, Pedersen S, Kurland CG. Effects of miaA on translation and growth rates. Mol Gen Genet 1987; 208:373-6; PMID:3312947; http://dx.doi.org/10.1007/BF00328126
   PubMedGoogle Scholar
• Ericson JU, Bjork GR. Pleiotropic effects induced by modification deficiency next to the anticodon of transfer-Rna from salmonella-typhimurium-Lt2. J Bacteriol 1986; 166:1013-21; PMID:2423501; http://dx.doi.org/10.1128/jb.166.3.1013-1021.1986
   PubMed Web of Science ®Google Scholar
• Bouadloun F, Srichaiyo T, Isaksson LA, Bjork GR. Influence of modification next to the anticodon in Transfer-Rna on codon context-sensitivity of translational suppression and accuracy. J Bacteriol 1986; 166:1022-7; PMID:3086285; http://dx.doi.org/10.1128/jb.166.3.1022-1027.1986
   PubMed Web of Science ®Google Scholar
• Diaz I, Ehrenberg M. Ms2i6a deficiency enhances proofreading in translation. J Mol Biol 1991; 222:1161-71; PMID:1762149; http://dx.doi.org/10.1016/0022-2836(91)90599-2
   PubMed Web of Science ®Google Scholar
• Urbonavicius J, Qian O, Durand JMB, Hagervall TG, Bjork GR. Improvement of reading frame maintenance is a common function for several tRNA modifications. Embo J 2001; 20:4863-73; PMID:11532950; http://dx.doi.org/10.1093/emboj/20.17.4863
   PubMed Web of Science ®Google Scholar
• Durand JMB, Bjork GR, Kuwae A, Yoshikawa M, Sasakawa C. The modified nucleoside 2-methylthio-N-6-isopentenyladenosine in tRNA of Shigella flexneri is required for expression of virulence genes. J Bacteriol 1997; 179:5777-82; PMID:9294434; http://dx.doi.org/10.1128/jb.179.18.5777-5782.1997
   PubMed Web of Science ®Google Scholar
• Duechler M, Leszczynska G, Sochacka E, Nawrot B. Nucleoside modifications in the regulation of gene expression: focus on tRNA. Cell Mol Life Sci 2016; 73:3075-95; PMID:27094388; http://dx.doi.org/10.1007/s00018-016-2217-y
   PubMed Web of Science ®Google Scholar
• Endres L, Dedon PC, Begley TJ. Codon-biased translation can be regulated by wobble-base tRNA modification systems during cellular stress responses. RNA Biol 2015; 12:603-14; PMID:25892531; http://dx.doi.org/10.1080/15476286.2015.1031947
   PubMed Web of Science ®Google Scholar
• Kolmsee T, Hengge R. Rare codons play a positive role in the expression of the stationary phase sigma factor RpoS (sigma(S)) in Escherichia coli. RNA Biol 2011; 8:913-21; PMID:21788735; http://dx.doi.org/10.4161/rna.8.5.16265
   PubMed Web of Science ®Google Scholar
• Thompson KM, Gottesman S. The MiaA tRNA modification enzyme is necessary for robust RpoS expression in Escherichia coli. J Bacteriol 2014; 196:754-61; PMID:24296670; http://dx.doi.org/10.1128/JB.01013-13
   PubMed Web of Science ®Google Scholar
• Aubee JI, Olu M, Thompson KM. The i6A37 tRNA modification is essential for proper decoding of UUX-Leucine codons during rpoS and iraP translation. RNA 2016; 22:729-42; PMID:26979278; http://dx.doi.org/10.1261/rna.053165.115
   PubMed Web of Science ®Google Scholar
• Martin NC, Hopper AK. Isopentenylation of both cytoplasmic and mitochondrial tRNA is affected by a single nuclear mutation. J Biol Chem 1982; 257:10562-5; PMID:7050116
   PubMed Web of Science ®Google Scholar
• Najarian D, Dihanich ME, Martin NC, Hopper AK. DNA sequence and transcript mapping of MOD5: features of the 5′ region which suggest two translational starts. Mol Cell Biol 1987; 7:185-91; PMID:3031457; http://dx.doi.org/10.1128/MCB.7.1.185
   PubMed Web of Science ®Google Scholar
• Slusher LB, Gillman EC, Martin NC, Hopper AK. mRNA leader length and initiation codon context determine alternative AUG selection for the yeast gene MOD5. Proc Natl Acad Sci U S A 1991; 88:9789-93; PMID:1946403; http://dx.doi.org/10.1073/pnas.88.21.9789
   PubMed Web of Science ®Google Scholar
• Gillman EC, Slusher LB, Martin NC, Hopper AK. MOD5 translation initiation sites determine N6-isopentenyladenosine modification of mitochondrial and cytoplasmic tRNA. Mol Cell Biol 1991; 11:2382-90; PMID:1850093; http://dx.doi.org/10.1128/MCB.11.5.2382
   PubMed Web of Science ®Google Scholar
• Boguta M, Hunter LA, Shen WC, Gillman EC, Martin NC, Hopper AK. Subcellular locations of MOD5 proteins: mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms commingle in the cytosol. Mol Cell Biol 1994; 14:2298-306; PMID:8139535; http://dx.doi.org/10.1128/MCB.14.4.2298
   PubMed Web of Science ®Google Scholar
• Tolerico LH, Benko AL, Aris JP, Stanford DR, Martin NC, Hopper AK. Saccharomyces cerevisiae Mod5p-II contains sequences antagonistic for nuclear and cytosolic locations. Genetics 1999; 151:57-75; PMID:9872948
   PubMed Web of Science ®Google Scholar
• Lamichhane TN, Arimbasseri AG, Rijal K, Iben JR, Wei FY, Tomizawa K, Maraia RJ. Lack of tRNA-i6A modification causes mitochondrial-like metabolic deficiency in S. pombe by limiting activity of cytosolic tRNATyr, not mito-tRNA. RNA 2016; 22:583-96; PMID:26857223; http://dx.doi.org/10.1261/rna.054064.115
   PubMed Web of Science ®Google Scholar
• Egel R, Kohli J, Thuriaux P, Wolf K. Genetics of the fission yeast Schizosaccharomyces pombe. Ann Rev Genet 1980; 14:77-108; PMID:7011176; http://dx.doi.org/10.1146/annurev.ge.14.120180.000453
   PubMed Web of Science ®Google Scholar
• Janner F, Vogeli G, Fluri R. The antisuppressor strain sin1 of Schizosaccharomyces pombe lacks the modification isopentenyladenosine in transfer RNA. J Mol Biol 1980; 139:207-19; PMID:7411631; http://dx.doi.org/10.1016/0022-2836(80)90305-8
   PubMed Web of Science ®Google Scholar
• Kohli J, Kwong T, Altruda F, Soll D, Wahl G. Characterization of a UGA-suppressing serine tRNA from Schizosaccharomyces pombe with the help of a new in vitro assay system for eukaryotic suppressor tRNAs. J Biol Chem 1979; 254:1546-51; PMID:762155
   PubMed Web of Science ®Google Scholar
• Rafalski A, Kohli J, Agris P, Soll D. The nucleotide sequence of a UGA suppressor serine tRNA from Schizosaccharomyces pombe. Nucleic Acids Res 1979; 6:2683-95; PMID:461200; http://dx.doi.org/10.1093/nar/6.8.2683
   PubMed Web of Science ®Google Scholar
• Lamichhane TN, Blewett NH, Maraia RJ. Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases. RNA 2011; 17:1846-57; PMID:21873461; http://dx.doi.org/10.1261/rna.2628611
   PubMed Web of Science ®Google Scholar
• Lamichhane TN, Blewett NH, Crawford AK, Cherkasova VA, Iben JR, Begley TJ, Farabaugh PJ, Maraia RJ. Lack of tRNA modification isopentenyl-A37 alters mRNA decoding and causes metabolic deficiencies in fission yeast. Mol Cell Biol 2013; 33:2918-29; PMID:23716598; http://dx.doi.org/10.1128/MCB.00278-13
   PubMed Web of Science ®Google Scholar
• Takahara T, Maeda T. TORC1 of fission yeast is rapamycin-sensitive. Genes Cells 2012; 17:698-708; PMID:22762302; http://dx.doi.org/10.1111/j.1365-2443.2012.01618.x
   PubMed Web of Science ®Google Scholar
• Lemieux J, Lakowski B, Webb A, Meng Y, Ubach A, Bussiere F, Barnes T, Hekimi S. Regulation of physiological rates in Caenorhabditis elegans by a tRNA-modifying enzyme in the mitochondria. Genetics 2001; 159:147-57; PMID:11560893
   PubMed Web of Science ®Google Scholar
• Lakowski B, Hekimi S. Determination of life-span in Caenorhabditis elegans by four clock genes. Science 1996; 272:1010-3; PMID:8638122; http://dx.doi.org/10.1126/science.272.5264.1010
   PubMed Web of Science ®Google Scholar
• Braeckman BP, Houthoofd K, De Vreese A, Vanfleteren JR. Apparent uncoupling of energy production and consumption in long-lived Clk mutants of Caenorhabditis elegans. Curr Biol 1999; 9:493-6; PMID:10330373; http://dx.doi.org/10.1016/S0960-9822(99)80216-4
   PubMed Web of Science ®Google Scholar
• Suzuki T, Nagao A, Suzuki T. Human mitochondrial tRNAs: biogenesis, function, structural aspects, and diseases. Annu Rev Genet 2011; 45:299-329; PMID:21910628; http://dx.doi.org/10.1146/annurev-genet-110410-132531
   PubMed Web of Science ®Google Scholar
• Fradejas N, Carlson BA, Rijntjes E, Becker NP, Tobe R, Schweizer U. Mammalian Trit1 is a tRNA([Ser]Sec)-isopentenyl transferase required for full selenoprotein expression. Biochem J 2013; 450:427-32; PMID:23289710; http://dx.doi.org/10.1042/BJ20121713
   PubMed Web of Science ®Google Scholar
• Lee BJ, Worland PJ, Davis JN, Stadtman TC, Hatfield DL. Identification of a selenocysteyl-tRNA(Ser) in mammalian cells that recognizes the nonsense codon, UGA. J Biol Chem 1989; 264:9724-7; PMID:2498338
   PubMed Web of Science ®Google Scholar
• Schweizer U, Fradejas-Villar N. Why 21? The significance of selenoproteins for human health revealed by inborn errors of metabolism. FASEB J 2016; 30(11):3669-81; PMID:27473727; http://dx.doi.org/10.1096/fj.201600424
   PubMed Web of Science ®Google Scholar
• Carlson BA, Novoselov SV, Kumaraswamy E, Lee BJ, Anver MR, Gladyshev VN, Hatfield DL. Specific excision of the selenocysteine tRNA[Ser]Sec (Trsp) gene in mouse liver demonstrates an essential role of selenoproteins in liver function. J Biol Chem 2004; 279:8011-7; PMID:14660662; http://dx.doi.org/10.1074/jbc.M310470200
   PubMed Web of Science ®Google Scholar
• Schweizer U, Streckfuss F, Pelt P, Carlson BA, Hatfield DL, Köhrle J, Schomburg L. Hepatically derived selenoprotein P is a key factor for kidney but not for brain selenium supply. Biochem J 2005; 386:221-6; PMID:15638810; http://dx.doi.org/10.1042/BJ20041973
   PubMed Web of Science ®Google Scholar
• Carlson BA, Schweizer U, Perella C, Shrimali RK, Feigenbaum L, Shen L, Speransky S, Floss T, Jeong SJ, Watts J, et al. The selenocysteine tRNA STAF-binding region is essential for adequate selenocysteine tRNA status, selenoprotein expression and early age survival of mice. Biochem J 2009; 418:61-71; PMID:18973473; http://dx.doi.org/10.1042/BJ20081304
   PubMed Web of Science ®Google Scholar
• Schoenmakers E, Carlson B, Agostini M, Moran C, Rajanayagam O, Bochukova E, Tobe R, Peat R, Gevers E, Muntoni F, et al. Mutation in human selenocysteine transfer RNA selectively disrupts selenoprotein synthesis. J Clin Invest 2016; 126:992-6; PMID:26854926; http://dx.doi.org/10.1172/JCI84747
   PubMed Web of Science ®Google Scholar
• Diamond AM, Choi IS, Crain PF, Hashizume T, Pomerantz SC, Cruz R, Steer CJ, Hill KE, Burk RF, McCloskey JA, et al. Dietary selenium affects methylation of the wobble nucleoside in the anticodon of selenocysteine transfer RNA[Ser]Sec. J Biol Chem 1993; 268:14215-23; PMID:8314785
   PubMed Web of Science ®Google Scholar
• Carlson BA, Moustafa ME, Sengupta A, Schweizer U, Shrimali R, Rao M, Zhong N, Wang S, Feigenbaum L, Lee BJ, et al. Selective restoration of the selenoprotein population in a mouse hepatocyte selenoproteinless background with different mutant selenocysteine tRNAs lacking Um34. J Biol Chem 2007; 282:32591-602; PMID:17848557; http://dx.doi.org/10.1074/jbc.M707036200
   PubMed Web of Science ®Google Scholar
• Warner GJ, Berry MJ, Moustafa ME, Carlson BA, Hatfield DL, Faust JR. Inhibition of selenoprotein synthesis by selenocysteine tRNA[Ser]Sec lacking isopentenyladenosine. J Biol Chem 2000; 275:28110-9; PMID:10821829
   PubMed Web of Science ®Google Scholar
• Howard MT, Carlson BA, Anderson CB, Hatfield DL. Translational redefinition of UGA codons is regulated by selenium availability. J Biol Chem 2013; 288:19401-13; PMID:23696641; http://dx.doi.org/10.1074/jbc.M113.481051
   PubMed Web of Science ®Google Scholar
• Ganichkin OM, Anedchenko EA, Wahl MC. Crystal structure analysis reveals functional flexibility in the selenocysteine-specific tRNA from mouse. PLoS One 2011; 6:e20032; PMID:21629646; http://dx.doi.org/10.1371/journal.pone.0020032
   PubMed Web of Science ®Google Scholar
• Cabello-Villegas J, Winkler ME, Nikonowicz EP. Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe). J Mol Biol 2002; 319:1015-34; PMID:12079344; http://dx.doi.org/10.1016/S0022-2836(02)00382-0
   PubMed Web of Science ®Google Scholar
• Weixlbaumer A, Murphy FV 4th, Dziergowska A, Malkiewicz A, Vendeix FA, Agris PF, Ramakrishnan V. Mechanism for expanding the decoding capacity of transfer RNAs by modification of uridines. Nat Struct Mol Biol 2007; 14:498-502; PMID:17496902; http://dx.doi.org/10.1038/nsmb1242
   PubMed Web of Science ®Google Scholar
• Smaldino PJ, Read DF, Pratt-Hyatt M, Hopper AK, Engelke DR. The cytoplasmic and nuclear populations of the eukaryote tRNA-isopentenyl transferase have distinct functions with implications in human cancer. Gene 2015; 556:13-8; PMID:25261850; http://dx.doi.org/10.1016/j.gene.2014.09.049
   PubMed Web of Science ®Google Scholar
• Spinola M, Galvan A, Pignatiello C, Conti B, Pastorino U, Nicander B, Paroni R, Dragani TA. Identification and functional characterization of the candidate tumor suppressor gene TRIT1 in human lung cancer. Oncogene 2005; 24:5502-9; PMID:15870694; http://dx.doi.org/10.1038/sj.onc.1208687
   PubMed Web of Science ®Google Scholar
• Torres AG, Batlle E, de Pouplana LR. Role of tRNA modifications in human diseases. Trends Mol Med 2014; 20:306-14; PMID:24581449; http://dx.doi.org/10.1016/j.molmed.2014.01.008
   PubMed Web of Science ®Google Scholar
• Yarham JW, Lamichhane TN, Pyle A, Mattijssen S, Baruffini E, Bruni F, Donnini C, Vassilev A, He L, Blakely EL, et al. Defective i6A37 modification of mitochondrial and cytosolic tRNAs results from pathogenic mutations in TRIT1 and its substrate tRNA. PLoS Genet 2014; 10:e1004424; PMID:24901367; http://dx.doi.org/10.1371/journal.pgen.1004424
   PubMed Web of Science ®Google Scholar
• Wei FY, Zhou B, Suzuki T, Miyata K, Ujihara Y, Horiguchi H, Takahashi N, Xie P, Michiue H, Fujimura A, et al. Cdk5rap1-mediated 2-methylthio modification of mitochondrial tRNAs governs protein translation and contributes to myopathy in mice and humans. Cell Metab 2015; 21:428-42; PMID:25738458; http://dx.doi.org/10.1016/j.cmet.2015.01.019
   PubMed Web of Science ®Google Scholar
• Steinthorsdottir V, Reynisdottir I, Thorleifsson G, Ghosh S, Benediktsson R, Sigurdsson G, et al. The recently identified type 2 diabetes gene CDKAL1 is widely expressed and its expression in pancreatic beta cells is affected by glucose concentration. Diabetologia 2007; 50(Suppl 1): S129; http://dx.doi.org/10.1007/s00125-007-0809-7
   Google Scholar
• Steinthorsdottir V, Thorleifsson G, Reynisdottir I, Benediktsson R, Jonsdottir T, Walters GB, Styrkarsdottir U, Gretarsdottir S, Emilsson V, Ghosh S, et al. A variant in CDKAL1 influences insulin response and risk of type 2 diabetes. Nat Genet 2007; 39:770-5; PMID:17460697; http://dx.doi.org/10.1038/ng2043
   PubMed Web of Science ®Google Scholar
• Wei FY, Suzuki T, Watanabe S, Kimura S, Kaitsuka T, Fujimura A, Matsui H, Atta M, Michiue H, Fontecave M, et al. Deficit of tRNA(Lys) modification by Cdkal1 causes the development of type 2 diabetes in mice. J Clin Invest 2011; 121:3598-608; PMID:21841312; http://dx.doi.org/10.1172/JCI58056
   PubMed Web of Science ®Google Scholar
• Thiaville PC, Iwata-Reuyl D, de Crecy-Lagard V. Diversity of the biosynthesis pathway for threonylcarbamoyladenosine (t(6)A), a universal modification of tRNA. RNA Biol 2014; 11:1529-39; PMID:25629598; http://dx.doi.org/10.4161/15476286.2014.992277
   PubMed Web of Science ®Google Scholar
• Rodriguez V, Chen Y, Elkahloun A, Dutra A, Pak E, Chandrasekharappa S. Chromosome 8 BAC array comparative genomic hybridization and expression analysis identify amplification and overexpression of TRMT12 in breast cancer. Genes Chromosomes Cancer 2007; 46:694-707; PMID:17440925; http://dx.doi.org/10.1002/gcc.20454
   PubMed Web of Science ®Google Scholar
• Chimnaronk S, Forouhar F, Sakai J, Yao M, Tron CM, Atta M, Fontecave M, Hunt JF, Tanaka I. Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon. Biochemistry 2009; 48:5057-65; PMID:19435325; http://dx.doi.org/10.1021/bi900337d
   PubMed Web of Science ®Google Scholar
• Seif E, Hallberg BM. RNA-protein mutually induced fit: structure of Escherichia coli isopentenyl-tRNA transferase in complex with tRNA(Phe). J Biol Chem 2009; 284:6600-4; PMID:19158097; http://dx.doi.org/10.1074/jbc.C800235200
   PubMed Web of Science ®Google Scholar
• Zhou C, Huang RH. Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: insight into tRNA recognition and reaction mechanism. Proc Natl Acad Sci U S A 2008; 105:16142-7; PMID:18852462; http://dx.doi.org/10.1073/pnas.0805680105
   PubMed Web of Science ®Google Scholar
• Moore JA, Poulter CD. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: A binding mechanism for recombinant enzyme. Biochemistry 1997; 36:604-14; PMID:9012675; http://dx.doi.org/10.1021/bi962225l
   PubMed Web of Science ®Google Scholar
• Liu W, Xie Y, Ma J, Luo X, Nie P, Zuo Z, Lahrmann U, Zhao Q, Zheng Y, Zhao Y, et al. IBS: an illustrator for the presentation and visualization of biological sequences. Bioinformatics 2015; 31:3359-61; PMID:26069263; http://dx.doi.org/10.1093/bioinformatics/btv362
   PubMed Web of Science ®Google Scholar
• Benko AL, Vaduva G, Martin NC, Hopper AK. Competition between a sterol biosynthetic enzyme and tRNA modification in addition to changes in the protein synthesis machinery causes altered nonsense suppression. Proc Natl Acad Sci U S A 2000; 97:61-6; PMID:10618371; http://dx.doi.org/10.1073/pnas.97.1.61
   PubMed Web of Science ®Google Scholar
• Kaminska J, Grabinska K, Kwapisz M, Sikora J, Smagowicz WJ, Palamarczyk G, Zoładek T, Boguta M. The isoprenoid biosynthetic pathway in Saccharomyces cerevisiae is affected in a maf1-1 mutant with altered tRNA synthesis. FEMS Yeast Res 2002; 2:31-7; PMID:12702319; http://dx.doi.org/10.1111/j.1567-1364.2002.tb00066.x
   PubMed Web of Science ®Google Scholar
• Moosmann B, Behl C. Selenoprotein synthesis and side-effects of statins. Lancet 2004; 363:892-4; PMID:15031036; http://dx.doi.org/10.1016/S0140-6736(04)15739-5
   PubMed Web of Science ®Google Scholar
• Ferreiro A, Quijano-Roy S, Pichereau C, Moghadaszadeh B, Goemans N, Bonnemann C, Jungbluth H, Straub V, Villanova M, Leroy JP, et al. Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: reassessing the nosology of early-onset myopathies. Am J Hum Genet 2002; 71:739-49; PMID:12192640; http://dx.doi.org/10.1086/342719
   PubMed Web of Science ®Google Scholar
• Ferreiro A, Ceuterick-de Groote C, Marks JJ, Goemans N, Schreiber G, Hanefeld F, Fardeau M, Martin JJ, Goebel HH, Richard P, et al. Desmin-related myopathy with Mallory body-like inclusions is caused by mutations of the selenoprotein N gene. Ann Neurol 2004; 55:676-86; PMID:15122708; http://dx.doi.org/10.1002/ana.20077
   PubMed Web of Science ®Google Scholar
• Moghadaszadeh B, Petit N, Jaillard C, Brockington M, Roy SQ, Merlini L, Romero N, Estournet B, Desguerre I, Chaigne D, et al. Mutations in SEPN1 cause congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Nat Genet 2001; 29:17-8; PMID:11528383; http://dx.doi.org/10.1038/ng713
   PubMed Web of Science ®Google Scholar
• Pratt-Hyatt M, Pai DA, Haeusler RA, Wozniak GG, Good PD, Miller EL, McLeod IX, Yates JR 3rd, Hopper AK, Engelke DR. Mod5 protein binds to tRNA gene complexes and affects local transcriptional silencing. Proc Natl Acad Sci U S A 2013; 110:E3081-9; PMID:23898186; http://dx.doi.org/10.1073/pnas.1219946110
   PubMed Web of Science ®Google Scholar
• Suzuki G, Shimazu N, Tanaka M. A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress. Science 2012; 336:355-9; PMID:22517861; http://dx.doi.org/10.1126/science.1219491
   PubMed Web of Science ®Google Scholar
• Yamaizumi Z, Kuchino Y, Harada F, Nishimura S, McCloskey JA. Primary structure of Escherichia coli tRNA UUR Leu. Presence of an unknown adenosine derivative in the first position of the anticodon which recognizes the UU codon series. J Biol Chem 1980; 255:2220-5; PMID:6986390
   PubMed Web of Science ®Google Scholar
• Barrell BG, Sanger F. The sequence of phenylalanine tRNA from E. coli. FEBS Lett 1969; 3:275-8; PMID:11947028; http://dx.doi.org/10.1016/0014-5793(69)80157-2
   PubMed Web of Science ®Google Scholar
• Ishikura H, Yamada Y, Nishimura S. The nucleotide sequence of a serine tRNA from Escherichia coli. FEBS Lett 1971; 16:68-70; PMID:11945903; http://dx.doi.org/10.1016/0014-5793(71)80688-9
   PubMed Web of Science ®Google Scholar
• Hirsh D. Tryptophan transfer RNA as the UGA suppressor. J Mol Biol 1971; 58:439-58; PMID:4933412; http://dx.doi.org/10.1016/0022-2836(71)90362-7
   PubMed Web of Science ®Google Scholar
• Goodman HM, Abelson JN, Landy A, Zadrazil S, Smith JD. The nucleotide sequences of tyrosine transfer RNAs of Escherichia coli. Eur J Biochem 1970; 13:461-83; PMID:4315419; http://dx.doi.org/10.1111/j.1432-1033.1970.tb00950.x
   PubMedGoogle Scholar
• Etcheverry T, Colby D, Guthrie C. A precursor to a minor species of yeast tRNASer contains an intervening sequence. Cell 1979; 18:11-26; PMID:389430; http://dx.doi.org/10.1016/0092-8674(79)90349-0
   PubMed Web of Science ®Google Scholar
• Madison JT, Kung HK. Large oligonucleotides isolated from yeast tyrosine transfer ribonucleic acid after partial digestion with ribonuclease T1. J Biol Chem 1967; 242:1324-30; PMID:6023574
   PubMed Web of Science ®Google Scholar
• Keith G, Roy A, Ebel JP, Dirheimer G. The nucleotide sequences of two tryptophane-tRNAs from brewer's yeast. FEBS Lett 1971; 17:306-8; PMID:11946053; http://dx.doi.org/10.1016/0014-5793(71)80171-0
   PubMed Web of Science ®Google Scholar
• Wilson RK, Roe BA. Presence of the hypermodified nucleotide N6-(delta 2-isopentenyl)-2-methylthioadenosine prevents codon misreading by Escherichia coli phenylalanyl-transfer RNA. Proc Natl Acad Sci U S A 1989; 86:409-13; PMID:2643111; http://dx.doi.org/10.1073/pnas.86.2.409
   PubMed Web of Science ®Google Scholar
• Bouadloun F, Srichaiyo T, Isaksson LA, Bjork GR. Influence of modification next to the anticodon in tRNA on codon context sensitivity of translational suppression and accuracy. J Bacteriol 1986; 166:1022-7; PMID:3086285; http://dx.doi.org/10.1128/jb.166.3.1022-1027.1986
   PubMed Web of Science ®Google Scholar
• Thiaville PC, Legendre R, Rojas-Benitez D, Baudin-Baillieu A, Hatin I, Chalancon G, Glavic A, Namy O, de Crécy-Lagard V. Global translational impacts of the loss of the tRNA modification t6A in yeast. Microbial Cell 2016; 3:29-45; PMID:26798630; http://dx.doi.org/10.15698/mic2016.01.473
   PubMed Web of Science ®Google Scholar
• Durant PC, Bajji AC, Sundaram M, Kumar RK, Davis DR. Structural effects of hypermodified nucleosides in the Escherichia coli and human tRNALys anticodon loop: the effect of nucleosides s2U, mcm5U, mcm5s2U, mnm5s2U, t6A, and ms2t6A. Biochemistry 2005; 44:8078-89; PMID:15924427; http://dx.doi.org/10.1021/bi050343f
   PubMed Web of Science ®Google Scholar
• Subramanian M, Srinivasan T, Sudarsanam D. Examining the Gm18 and m(1)G Modification Positions in tRNA Sequences. Genomics Inform 2014; 12:71-5; PMID:25031570; http://dx.doi.org/10.5808/GI.2014.12.2.71
   PubMedGoogle Scholar
• Wang M, Peng Y, Zheng J, Zheng B, Jin X, Liu H, Wang Y, Tang X, Huang T, Jiang P, et al. A deafness-associated tRNAAsp mutation alters the m1G37 modification, aminoacylation and stability of tRNAAsp and mitochondrial function. Nucleic Acids Res 2016; 44:10974-85; PMID:27536005; http://dx.doi.org/10.1093/nar/gkw726
   PubMed Web of Science ®Google Scholar
• Tuorto F, Lyko F. Genome recoding by tRNA modifications. Open Biol 2016; 6:pii: 160287; PMID:27974624; http://dx.doi.org/10.1098/rsob.160287
   PubMed Web of Science ®Google Scholar
• Waas WF, Druzina Z, Hanan M, Schimmel P. Role of a tRNA base modification and its precursors in frameshifting in eukaryotes. J Biol Chem 2007; 282:26026-34; PMID:17623669; http://dx.doi.org/10.1074/jbc.M703391200
   PubMed Web of Science ®Google Scholar