Abstract
Three classes of point mutations occur in nature: (1) missense; (2) nonsense; and (3) frameshift. Aminoacyl-tRNAs, which suppress mutations within each class, have been characterized in microorganisms; excellent reviews covering these studies have been published (Eggertsson and Sö11 1988; Hill 1975; Körner et al. 1978; Murgola 1985, 1989; Sherman 1982; Smith 1979; Steege and Söll 1979). The aminoacyl-tRNAs involved in suppression of point mutations are called missense, nonsense, and frameshift suppressors. Nonsense suppressors are further classified as amber, ochre, and opal when they suppress UAG, UAA, and UGA codons, respectively. Even though our understanding of the occurrence, structure, and function of suppressor tRNAs in mammalian cells is largely just beginning to emerge, it would seem that our interpretation of the role of suppressor tRNAs in mammalian cells may have to be altered from the classical viewpoint. That is, in microorganisms, suppressor tRNAs have largely been thought of as providing a mechanism of correcting or reversing deleterious mutations. It appears that suppressor tRNAs, when they occur in mammalian cells, have specialized functions and are not present in order to reverse the effect of deleterious mutations.
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Keywords
- Termination Codon
- Equine Infectious Anemia Virus
- Beet Necrotic Yellow Vein Virus
- Anticodon Loop
- Nonsense Suppression
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
Barbacid M (1987) Ras genes. Annu Rev Biochem 56:779–827
Barciszewski J, Barciszewski M, Suter B, Kubli E (1985) Plant tRNA suppressors: in vivo readthrough properties and nucleotide sequence of yellow lupin seeds tRNAtYr. Plant Sci 40: 193–196
Baserga SJ, Benz EJ Jr (1988) Nonsense mutations in the human beta-globin gene affect mRNA metabolism. Proc Natl Acad Sci USA 85: 2056–2060
Beier H, Barciszewski M, Krupp G, Mitnacht R, Gross HJ (1984a) UAG readthrough during TMV RNA translation: isolation and sequence of two tRNAstY with suppressor activity from tobacco plants. EMBO J 3: 351–356
Beier H, Barciszewski M, Sickinger H-D (1984b) The molecular basis for the differential translation of TMV RNA in tobacco protoplasts and wheat germ extracts. EMBO J 3: 1091–1096
Bienz M, Kubli E (1981) Wild-type tRNATY/G reads the TMV RNA stop codon, but Q base-modified tRNATYr/Q does not. Nature 294: 188–190
Bienz M, Kubli E, Kohli J, de Henau S, Grosjean H (1980) Nonsense suppression in eukaryotes: the use of the Xenopus oocyte as an in vivo assay system. Nucleic Acids Research 8: 5169–5178
Bienz M, Kubli E, Kohli J, de Henau S, Huez G, Marbaix G, Grosjean H (1981) Usage of three termination codons in a single eukaryotic cell, the Xenopus oocyte, Nucleic Acids Research 9: 3835–3850
Björk GR, Erickson JU, Gustafsson CED, Hagervall TG, Jönsson YH, Wilkström PM (1987) Transfer RNA Modification. Annu Rev Biochem 56: 263–287
Böck A, Stadtman TC (1988) Selenocysteine, a highly specific component of certain enzymes, is incorporated by a UGA-directed co-translational mechanism. Biofactors 1: 245–250
Bossi L (1983) Context effects: translation of UAG codon by suppressor tRNA is affected by the sequence following UAG in the message. J Mol Biol 164: 73–87
Brierly I, Boursnell ME, Binns MM, Bilimoria B, Block VC, Brown TDK, Inglis SC (1987) An efficient ribosomal frameshifting signal in the polymerase-encoding region of the corona-virus IBV. EMBO J 6: 3779–3785
Bunn HF, Forget BG (1986) Hemoglobin: molecular, genetics and clinical aspects. Sanders, Philadelphia USA
Capecchi MR, Vonder Haar RA, Capecchi NE, Sveda MM (1977) The isolation of a suppressible nonsense mutant in mammalian cells. Cell 12: 371–381
Role of Nonsense, Frameshift, and Missense Suppressor tRNAs in Mammalian Cells 139
Capone JP, Sharp PA, RajBhandary UL (1985) Amber, ochre and opal suppressor tRNA genes derived from a human serine tRNA gene. EMBO J 4: 213–221
Capone JP, Sedivy JM, Sharp PA, RajBhandary UL (1986) Introduction of UAG, UAA, and UGA nonsense mutations at a specific site in the Escherichia colt chloramphenicol acetyltransferase gene: use in measurement of amber, ochre, and opal suppression in mammalian cells. Mol Cell Biol 6: 3059–3067
Celis JE, Piper PW (1981) Nonsense suppressors in eukaryotes. Trends Biochem Sci 6: 177–179
Chakrabarti L, Guyader M, Alizon M, Daniel MD, Desrosiers RC, Tiollais P, Sonigo P (1987) Sequence of simian immunodeficiency virus from macaque and its relationship to other human and simian retroviruses. Nature 328: 543–547
Chambers I, Harrison PR (1987) A new puzzle in selenoprotein biosynthesis: selenocysteine seems to be encoded by the ‘stop’ codon, UGA. Trends Biochem Sci 12: 255–256
Chambers I, Frampton J, Goldfarb P, Affara N, McBain W, Harrison PR (1986) The structure of the mouse gluthione peroxidase gene: the selenocysteine in the active site is encoded by the `termination’ codon, TGA. EMBO J 5: 1221–1227
Chen S-H, Habib G, Yang C-Y, Gu Z-W, Lee BR, Weng S-A, Silberman SS, Cai S-J, Deslypere JP, Rosseneu M, Gotto AM Jr, Li W-H, Chan L (1987) Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon. Science 238: 363–366
Craigan WJ, Caskey CT (1987) Translational frameshifting: where will it stop? Cell 50: 1–2
Cremer KJ, Bodemer M, Summers WP, Summers WC, Gesteland RF (1979) In vitro suppression of UAG and UGA mutants in the thymidine kinase gene of Herpes simplex virus. Proc Natl Acad Sci USA 76: 430–434
Crick FHA (1966) Codon-anticodon pairing: the wobble hypothesis. J Mol Biol 19: 548–555
Davidson NO, Powell LM, Wallis SC, Scott J (1988) Thyroid hormone modulates the introduction of a stop codon in rat liver apolipoprotein B messenger RNA. J Biol Chem 263: 13482–13485
Dayhuff TJ, Atkins JF, Gesteland RF (1986) Characterization of ribosomal frameshift events by protein sequence analysis. J Biol Chem 261: 7491–7500
Diamond A, Dudock B, Hatfield D (1981) Structure and properties of a bovine liver UGA suppressor serine tRNA with a tryptophan anticodon. Cell 25: 497–506
Efstratiadis A, Kafatos F, Maniatis T (1977) The primary structure of rabbit ß-globin mRNA as determined from cloned DNA. Cell 10: 571–585
Eggertsson G, Söll D, (1988) Transfer ribonucleic acid-mediated suppression of termination codons. Microbiol Rev 52: 354–374
Engelberg-Kulka H, Schoulaker-Schwarz R (1988a) Stop is not the end: physiological implications of translational readthrough. J Theor Biol 131: 477–485
Engelberg-Kulka H, Schoulaker-Schwarz R (1988b) A flexible genetic code, or why does selenocysteine have no unique codon? Trends Biochem Sci 13: 419–421
Feng Y-X, Dong L, Zhang Y (1986) Homogeneous sequence in the anticodon of natural UAG suppressor tRNATYr. Acta Biochim Biophys Sinica 18: 90–95
Feng Y-X, Hatfield D, Rein A, Levin JG (1989a) Translational readthrough of the murine leukemia virus gag gene amber codon does not require virus-induced alteration of tRNA. J Virol 63: 2405–2410
Feng Y-X, Levin J, Hatfield D, Schaefer T, Gorelick R, Rein A (1989b) Suppression of UAA and UGA termination codons in mutant murine leukemia virus. J Virol 63: 2870–2873
Franchini G, Gurgo C, Guo H-G, Gallo RC, Collalti E, Fragnoli KA, Hall LF, Wong-Stahl F, Reitz MS (1987) Sequence of simian immunodeficiency virus and its relationship to the human immunodeficiency viruses. Nature 328: 539–543
Geller AI, Rich A (1980) UGA termination suppression tRNAT`P active in rabbit reticulocytes. Nature 283: 41–46
Gesteland R, Wills N (1979) Use of yeast suppressors for identification of adenovirus nonsense mutants. In: Celis JE, Smith JD (eds) Nonsense mutations and tRNA suppressors. Academic Press, London, pp 277–284
Gesteland RF, Wills N, Lewis JB, Grodzicker T (1977) Identification of amber and ochre mutants of the human virus Ad2 + ND1. Proc Natl Acad Sci USA 74: 4567–4571
Guyader M, Emerman M, Sonigo P, Clavel F, Montagnier L, Alizon M (1987) Genome organization and transactivation of the human immunodeficiency virus type 2. Nature 326: 662–669
Hardman DA, Protter AA, Schilling JW, Kane JP (1987) Carboxyl terminal analysis of human B-48 protein confirms the novel mechanism proposed for chain termination. Biochem Biophys Res Commun 149: 1214–1219
Harley CB, Pollard JW, Stanners CP, Goldstein S (1981) Model for messenger RNA translation during amino acid starvation applied to the calculation of protein synthetic error rates. J Biol Chem 156: 10786–10794
Hatfield D (1972) Recognition of nonsense codons in mammalian cells. Proc Natl Acad Sci USA 69: 3014–3018
Hatfield D (1985) Suppression of termination codons in higher eukaryotes. Trends Biochem Sci 10: 201–204
Hatfield D, Nirenberg M (1971) Binding of radioactive oligonucleotides to ribosomes Biochemistry 10: 4318–4323
Hatfield D, Portugal FH (1970) Seryl-tRNA in mammalian tissues: chromatographic differences in brain and liver and a specific response to the codon UGA. Proc Natl Acad Sci USA 67: 1200–1206
Hatfield D, Rice M (1986) Aminoacyl-tRNA (anticodon): codon adaptation in human and rabbit reticulocytes. Biochem Int 13: 835–842
Hatfield D, Matthews CR, Rice M (1979) Aminoacyl-transfer RNA populations in mammalian cells: chromatographic profiles and patterns of codon recognition. Biochim Biophys Acta 564: 414–423
Hatfield D, Diamond A, Dudock B (1982a) Opal suppressor serine tRNAs from bovine liver form phosphoseryl-tRNA. Proc Natl Acad USA 79: 6215–6219
Hatfield D, Varricchio F, Rice M, Forget BG (1982b) The aminoacyl-tRNA population of human reticulocytes. J Biol Chem 257: 3183–3188
Hatfield D, Dudock BS, Eden FC (1983) Characterization and nucleotide sequence of a chicken gene encoding an opal suppressor tRNA and its flanking DNA segments. Proc Natl Acad Sci USA 80: 4940–4944
Hatfield D, Thorgeirsson SS, Copeland TD, Oroszlan S, Bustin M (1988) Immunopurification of the suppressor tRNA dependent rabbit beta-globin readthrough protein. Biochemistry 27: 1179–1183
Hatfield D, Feng Y-X, Lee BJ, Rein A, Levin JG, Oroszlan S (1989) Chromatographic analysis of aminoacyl-tRNAs which are required for translation of codons at and around the ribosomal frameshift sites in HIV, HTLV-I, and BLV. Virology 173: 736–742
Hatfield D, Smith DWE, Lee BJ, Worland PJ, Oroszlan S (1989) Structure and function of suppressor tRNAs in higher eukaryotes. CRC critical reviews in biochemistry. CRC Press
Herr W (1984) Nucleotide sequence of AKV murine leukemia virus. J Virol 49: 471–478
Higuchi K, Hospattankar AV, Law SW, Meglin N, Cortright J, Brewer HB Jr (1988) Human apolipoprotein B (apoB) mRNA: identification of two distinct apoB mRNAs, an mRNA with the apo-B-100 sequence and an apoB mRNA containing a premature in-frame translational stop codon, in both liver and intestine. Proc Natl Acad Sci USA 85: 1772–1776
Hill CW (1975) Informational suppression of missense mutations. Cell 6: 419–427
Hiramatsu K, Nishida J, Naito A, Yoshikura H (1987) Molecular cloning of the closed circular provirus of human T cell leukemia virus type I: a new open reading frame in the gag-pol region. J Gen Virol 68: 213–218
Hizi A, Henderson LE, Copeland TD, Sowder RC, Hixson CV, Oroszlan S (1987) Characterization of mouse tumor virus gag-pol gene products and the ribosomal frameshift site by protein sequencing. Proc Natl Acad Sci USA 84: 7041–7045
Ho Y-S, Kan YW (1987) In vivo aminoacylation of human and Xenopus suppressor tRNAs constructed by site-specific mutagenesis. Proc Natl Acad Sci USA 84: 2185–2188
Ho Y-S, Norton GP, Palese P, Dozy AM, Kan YW (1986) Expression and function of suppressor tRNA genes in mammalian cells. Cold Spring Harbor Symposium on Quantitative Biology vol 51, Cold Spring Harbor, New York, pp 1033–1040
Hudziak RM, Laski FA, RajBhandary UL, Sharp PA, Capecchi MR (1982) Establishment of Role of Nonsense, Frameshift, and Missense Suppressor tRNAs in Mammalian Cells 141 mammalian cell lines containing multiple nonsense mutations and functional suppressor tRNA genes. Cell 31: 137–146
Inoue J-I, Watanabe T, Sato M, Oda A, Toyoshima K, Yoshida M, Seiki M (1986) Nucleotide sequence of the protease-coding region in an infectious DNA of simian retrovirus (STLV) of the HTLV-1 family. Virology 150: 187–195
Ishikawa M, Meshi T, Motoyoshi F, Takamatsu N, Okada Y (1986) In vitro mutagenesis of the putative replicase genes of tobacco mosaic virus. Nucleic Acids Res 14: 8291–8305
Jacks T, Varmus HE (1985) Expression of the Rous sarcoma virus pol gene by ribosomal frameshifting. Science 230: 1237–1242
Jacks T, Townsley K, Varmus HE, Majors J (1987) Two efficient ribosomal frameshifting events are required for synthesis of mouse mammary tumor virus gag-related polyproteins. Proc Natl Acad Sci USA 84: 4298–4302
Jacks T, Madhani HD, Masiraz FR, Varmus HE (1988a) Signals for ribosomal frameshifting in the Rous sarcoma virus gag-pol region. Cell 55: 447–458
Jacks T, Power MD, Masiarz FR, Luciw PA, Barr PJ, Varmus H (1988b) Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature 331: 280–283
Jackson RJ, Hunt T (1983) Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA. Methods Enzymol 96: 50–74
Jank P, Shindo-Okada N, Nishimura S, Gross HJ (1977) Rabbit liver tRNA: primary structure and unusual codon recognition. Nucletic Acids Res 4: 1999–2008
Johnson PF, Abelson J (1983) The yeast tRNATY gene intron is essential for correct modification of its tRNA product. Nature 302: 681–687
Kato N, Hoshino H, Harada F (1983) Minor serine tRNA containing anticodon NCA(C4 RNA) from human and mouse cells. Biochem Int 7: 635–645
Kawakami T, Sherman L, Dahlberg J, Gazit A, Yaniv A, Tronick SR, Aaronson SA (1987) Nucleotide sequence analysis of equine infectious anemia virus proviral DNA. Virology 158: 300–312
Kohli J, Grosjean H (1981) Usage of the three termination codons: compilation and analysis of known eukaryotic and prokaryotic translation termination sequences. Mol Gen Genet 182: 430–439
Kohli J, Kwong T, Altruda F, Söll D (1979) 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 254: 1546–1551
Körner AM, Freinstein SI, Altman S (1978) Transfer RNA-mediated suppression. In: Altman S (ed) Transfer RNA. MIT Press, Cambridge, pp 105–135
Kubli E, Schmidt T, Martin PF, Sofer W (1982) In vitro suppression of a nonsense mutant of Drosophila melanogaster. Nucleic Acids Res 10: 7145–7152
Kuchino Y, Borek E, Grunberger D, Mushinski J, Nishimura S (1982) Changes of post-transcriptional modification of Wye base in tumor-specific tRNAPh`. Nucleic Acids Res 10: 6421–6432
Kuchino Y, Beier H, Akita N, Nishimura S (1987) Natural UAG suppressor glutamine tRNA is elevated in mouse cells infected with Moloney murine leukemia virus. Proc Natl Acad Sci USA 84: 2668–2672
Kuchino Y, Nishimura S, Schröder HC, Rottmann M, Müller WEG (1988) Selective inhibition of formation of suppressor glutamine tRNA in Moloney murine leukemia virus-infected NIH-3T3 cells by Avarol. Virology 165: 518–526
Laski FA, Belagaje R, RajBhandary UL, Sharp PA (1982) An amber suppressor tRNA gene derived by site-specific mutagenesis: cloning and function in mammalian cells. Proc Natl Acad Sci USA 79: 5813–5817
Laski FA, Belagaje R, Hudziak RM, Capecchi MR, Norton GP, Palese P, RajBhandary UL, Sharp PA (1984) Synthesis of an ochre suppressor tRNA gene and expression in mammalian cells. EMBO J 3: 2445–2452
Lee BJ, Kang SG, Hatfield D (1989a) Transcription of Xenopus selenocysteyl-tRNAs (formerly designated opal suppressor phosphoserine tRNA) is directed by mutiple 5’ extra-genic regulatory elements. J Biol Chem 264: 9696–9702
Lee BJ, de la Peria P, Tobian JA, Zasloff M, Hatfield D (1987) Unique pathway of expression of an opal suppressor phosphoserine tRNA. Proc Natl Acad Sci USA 84: 6384–6388
Lee BJ, Worland PJ, Davis J, Stadium TC, Hatfield D (1989b) Identification of a selenocysteyl-tRNAser in mammalian cells which recognizes the nonsense codon, UGA. J Biol Chem 264: 9724–9727
Lehrman MA, Goldstein JL, Brown MS, Russell DW, Schneider WJ (1985) Internalization-defective LDL receptors produced by genes with nonsense and frameshift mutations that truncate the cytoplasmic domain. Cell 41: 735–743
Leinfelder W, Zehelein E, Mandrand-Berthelot M-A, Böck A (1988) Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature 331: 723–725
Leinfelder W, Stadtman TC, Böck A (1989) Occurrence in vivo of selenocysteyl-tRNASe’ in Escherichia coli: effect of sel mutants. J Biol Chem 264: 9720–9723
Li G, Rice CM (1989) Mutagenesis of the in-frame opal termination codon preceeding nsP4 of Sindbis virus: studies of translational readthrough and its effect on virus replication. J Virol 63: 1326–1337
Lin JP, Aker M, Sitney KC, Mortimer RL (1986) First position wobble in codon-anticodon pairing: amber suppression by a yeast glutamine tRNA. Gene 49: 383–388
Mäenpää PH (1972) Seryl transfer RNA alterations during estrogen-induced phosvitin synthesis: quantitative assay of the hormone-responding species by ribosomal binding. Biochem Biophys Res Commun 47: 971–974
Mäenpää PH, Bernfield MR (1970) A specific hepatic transfer RNA for phosphoserine. Proc Natl Acad Sci USA 67: 688–695
Marlor RL, Parkhurst SM, Corces VG (1986) The Drosophila melanogaster gypsy transposable elements encodes putative gene products homologous to retroviral proteins. Mol Cell Biol 6: 1129–1134
Marotta C, Wilson J, Forget BG, Weissman S (1977) Human globin messenger RNA: nucleotide sequences derived from complementary DNA. J Biol Chem 252: 5040–5053
McAdam RA, Goundis D, Reid KBM (1988) A homozygous point mutation results in a stop codon in the CIgB-chain of a Clq-deficient individual Immunogenetics 27: 259–264
McBride OW, Rajagopalan M, Hatfield D (1987) Opal suppressor phosphoserine tRNA gene and pseudogene are located on human chromosomes 19 and 22, respectively. J Biol Chem 262: 11163–11166
McBride OW, Mitchell A, Lee BJ, Mullenbach G, Hatfield D (1988) Gene for selenium-dependent glutathione peroxidase maps to human chromosomes 3, 21, and X. BioFactors 1: 285–292
Meier F, Suter B, Grosjean H, Keith G, Kubli E (1985) Queuosine modification of the wobble base in tRNA’s influences in vivo decoding properties. EMBO J 4: 823–827
Mietz JA, Grossman Z, Lueders KK, Kuff EL (1987) Nucleotide sequence of a complete mouse intracisternal A-particle genome: relationship to known aspects of particle assembly and function. J Virol 61: 3020–3029
Miller JH, Albertini AM (1983) Effects of surrounding sequence on the suppression of nonsense codons. J Mol Biol 164: 59–71
Mizutani T, Hashimoto A (1984) Purification and properties of suppressor seryl-tRNA: ATP phosphotransferase from bovine liver. FEBS Lett 169: 319–322
Mizutani T, Hitaka T (1988) Stronger affinity of reticulocyte release factor than natural suppressor tRNAse’ for the opal termination codon. FEBS Lett 226: 227–231
Mizutani T, Tachibana Y (1986) Possible incorporation of phosphoserine into globin readthrough protein via bovine opal suppressor phosphoseryl-tRNA. FEBS Lett 207: 162–166
Mizutani T, Narihara T, Hashimoto A (1984) Purification and properties of bovine liver seryltRNA synthetase. Eur J Biochem 143: 9–13
Mizutani T, Kanbe K, Kimura Y, Tachibana Y, Hitaka T (1988) Non-partition of opal suppressor phosphoseryl-transfer ribonucleic acid (tRNA) in phosphoserine aminotransferase catalysis. Chem Pharm Bull 36: 824–827
Moore R, Dixon M, Smith R, Peters G, Dickson C (1987) Complete nucleotide sequence of a milk-transmitted mouse mammary tumor virus: two frameshift suppression events are required for translation of gag and pol. J Virol 61: 480–490
Role of Nonsense, Frameshift, and Missense Suppressor tRNAs in Mammalian Cells 143
Mullenback GT, Tabrizi A, Irvine BD, Bell GI, Hallewell RA (1987) Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine. Nucleic Acids Res 15: 5484
Mullenback GT, Tabrizi A, Irvine BD, Bell GI, Tainer JA, Hallewell RA (1988) Selenocysteine’s mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases. Protein Engineer 2: 239–246
Müller WEG, Schröder HC, Reuter P, Sarin PS, Hess G, Meyer zum Büschenfelde K-H, Kuchino Y, Nishimura S (1988) Inhibition of expression of natural UAG suppressor glutamine tRNA in HIV-infected human H9 cells in vitro by Avarol. AIDS Res Human Retrovir 4: 279–286
Murgola EJ (1985) tRNA, suppression, and the code. Annu Rev Genet 19:57–80
Murgola EJ (1989) Mutant glycine tRNAs and other wonders of translation suppression. In: Cherayil JD (ed) Transfer RNAs and other soluble RNAs. CRC Press, Boca Raton
Murphy EC Jr, Wills N, Arlinghaus RB (1980) Suppression of murine retrovirus polypeptide termination: effect of amber suppressor tRNA on the cell-free translation of Rauscher murine leukemia virus, Moleney murine leukemia virus, and Moloney murine sarcoma virus 124 RNA. J Virol 34: 464–473
Nam SH, Kidokoro M, Shida H, Hatanka M (1988) Processing of gag precursor polyprotein of human T-cell leukemia virus type I by virus-encoded protease. J Virol 62: 3718–3728
Nirenberg M, Leder P (1964) RNA codewords and protein synthesis: the effect of trinculeotides upon the binding of sRNA to ribosomes. Science 145: 1399–1407
O’Neill VA, Eden FC, Pratt K, Hatfield D (1985) A human opal suppressor tRNA gene and pseudogene. J Biol Chem 260: 2501–2508
Panganiban AT (1988) Retroviral gag gene amber codon suppression is caused by an intrinsic cis-acting component of the viral mRNA. J Virol 62: 3574–3580
Parker J, Pollard JW, Friesen JD, Stanners CP (1978) Stuttering: high-level mistranslation in animal and bacterial cells. Proc Natl Acad Sci USA 75: 1091–1095
Pelham HRB (1978) Leaky UAG termination codon in tobacco mosaic virus RNA. Nature 272: 469–471
Philipson L, Andersson P, Olshevsky U, Weinberg R, Baltimore D (1978) Translation of MuLV and MSV RNAs in nuclease-treated reticulocyte extracts: enhancement of the gag-pol polypeptide with yeast suppressor tRNA. Cell 13: 189–199
Pollard J, Harley CB, Chamberlin JW, Goldstein S, Stanners CP (1982) Is transformation associated with an increased error frequency in mammalian cells? J Biol Chem 257: 5977–5979
Powell LM, Wallis SC, Pease RJ, Edwards YH, Knott TJ, Scott J (1987) A novel form of tissue- specific RNA processing produces apolipoprotein-B48 in intestine. Cell 50: 831–840
Power MD, Marx PA, Bryant ML, Gardner MB, Barr PJ, Luciw PA (1986) Nucleotide sequence of SRV-1, a type D simian acquired immune deficiency syndrome retrovirus. Science 231: 1567–1572
Pratt K, Eden FC, You KH, O’Neill VA, Hatfield D (1985) Conserved sequences in both coding and 5’ flanking regions of mammalian opal suppressor tRNA genes. Nucleic Acids Res 13: 4765–4775
Pure GA, Robinson GW, Naumovski L, Friedberg EC (1985) Partial suppression of an ochre mutation in Saccharomyces cerevisiae by multicopy plasmids containing a normal yeast tRNAG’ gene. J Mol Biol 183: 31–42
Raba M, Limberg K, Burghagen M, Katze JR, Simsek M, Heckman JE, RajBhandary UL, Gross HJ (1979) Nucleotide sequence of three isoaccepting lysine tRNAs from rabbit liver and SV40-transformed mouse fibroblast. Eur J Biochem 97: 305–318
Ratner L, Haseltine W, Patarca R, Livak KJ, Starcich B, Josephs SF, Doran ER, Rafalski JA, Whitehorn EA, Baumeister K, Ivanoff J, Petteway SR, Pearson ML, Lautenberger JA, Papas TS, Ghrayeb J, Chang NT, Gallo RC, Wong-Staal F (1985) Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature 313: 277–284
Reddy AP, Hsu BL, Reddy PS, Li N-Q, Thyagaraju K, Reddy CC, Tam MF, Tu C-PD (1988) Expression of glutathione peroxidase I gene in selenium-deficient rats. Nucleic Acids Res 16: 5557–5568
Rice N R, Stephens R, Burny A, Gilden R (1985) The gag and pol genes of bovine leukemia virus: nucleotide sequence and analysis. Virology 142: 357–377
Roberts BE, Paterson BM (1973) Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ. Proc Natl Acad Sci USA 70: 2330–2334
Romeo G. Hassan HJ, Staempfli S, Roncuzzi L, Cianetti L, Leonardi A, Vicente V, Mannucci PM, Bertina R, Peschle C, Cortese R (1987) Hereditary thrombophilia: identification of nonsense and missense mutations in the protein C gene. Proc Natl Acad Sci USA 84: 2829–2832
Sagata N, Yasunaga T, Tsuzuku-Kawamura J, Ohishi K, Ogawa Y, Ikawa Y (1985) Complete nucleotide sequence of the genome of bovine leukemia virus: its evolutionary relationship to other retroviruses. Proc Natl Acad Sci USA 82: 677–681
Saigo K, Kugiyama W, Matsuo Y, Inouye S, Yoshioka K, Yuki S (1984) Identification of the coding sequence for a reverse transcriptase-like enzyme in a transposable genetic element in Drosophila melanogaster. Nature 312: 659–663
Sanchez-Pescador R, Power MD, Barr PJ, Steimer KS, Stempien MM, Brown-Shimer SL, Gee WW, Renard A, Randolph A, Levy JA, Dina D, Luciw PA (1985) Nucleotide sequence and expression of AIDS-associated retrovirus (ARV-2). Science 227: 484–492
Satoh K, Nukiwa T, Brantly M, Garver RI Jr, Hofker M, Courtney M, Crystal RG (1988) Emphysema associated with complete absence of al-antitrypsin of a stop codon in an alantitrypsin-coding exon. Am J Human Genet 42: 77–83
Schwartz DE, Tizard R, Gilbert W (1983) Nucleotide sequence of Rous sarcoma virus. Cell 32: 853–869
Sedivy JM, Capone JP, RajBhandary UL, Sharp PA (1987) An inducible mammalian amber suppressor: propagation of a poliovirus mutant. Cell 50: 379–389
Seiki M, Hattori S, Hirayama Y, Yoshida M (1983) Human adult T-cell leukemia virus: complete nucleotide sequence of the provirus genome integrated in leukemia cell DNA. Proc Natl Acad Sci USA 80: 3618–3622
Sharp SJ, Stewart TS (1977) The characterization of phosphoseryl tRNA from lactating bovine mammary gland. Nucleic Acids Res 4: 2123–2136
Sherman F (1982) Suppression in yeast Saccharomyces cerevisiae. In: Strathern JN, Jones EW, Broach JR (eds) Molecular biology of the yeast Saccharomyces; metabolism and gene expression. Cold Spring Harbor Laboratories, New York, pp 463–486
Shimotohno K, Takahashi Y, Shimizu N, Gojobori T, Golde DW, Chen IS, Miwa M, Sugimura T (1985) Complete nucleotide sequence of an infectious clone of human T-cell leukemia virus type II: an open reading frame for the protease gene. Proc Natl Acad Sci USA 82: 3101–3105
Shindo-Okada N, Akimoto H, Nomura H, Nishmura S (1985) Recognition of UAG termination codon by mammalian tyrosine tRNA containing 6-thioqueuine in the first position of the anticodon. Proc Jpn Acad 61: 94–98
Shinnick TM, Lerner RA, Sutclife JG (1981) Nucleotide sequence of Moloney murine leukemia virus. Nature 293: 543–548
Smith DWE, Hatfield D (1986) Effects of post-translational base modifications on the site- specific function of transfer RNA in eukaryote translation. J Mol Biol 189: 663–671
Smith DWE, McNamara AL (1982) The effect of the Q base modification on the usage of tRNAH’s in globin synthesis. Biochem Biophys Res Commun 104: 1459–1463
Smith DWE, McNamara A, Rice M, Hatfield D (1981) The effects of a post-transcriptional modification on the function of tRNA isoaccepting species in translation. J Biol Chem 256: 10033–10036
Smith DWE, McNamara AL, Mushinski JF, Hatfield DL (1985) Tumor-specific, hypomodified phenylalanyl-tRNA is utilized in translation in preference to the fully modified isoacceptor of normal cells. J Biol Chem 260: 147–151
Smith JD (1979) Suppressor tRNAs in prokaryotes. In: Celis JE, Smith JD (eds) Nonsense mutations and tRNA suppressors. Academic Press, London pp 109–125
Sonigo P, Alizon M, Staskus K, Klatzmann D, Cole S, Danos O, Retzel E, Tiollais O, Haase A, Wain-Hobson S (1985) Nucleotide sequence of the visna lentivirus: relationship to the AIDS virus. Cell 42: 369–382
Role of Nonsense, Frameshift, and Missense Suppressor tRNAs in Mammalian Cells 145
Sonigo P, Barker C, Hunter E, Wain-Hobson S (1986) Nucleotide sequence of Mason-Pfizer monkey virus: an immunosuppressive D-type retrovirus. Cell 45: 375–385
Sprinzl M, Hartmann T, Meissner F, Moll J, Vorderwülbecke T (1987) Compilation of tRNA sequences and tRNA genes. Nucleic Acids Res (Sequences supplement) 15: 53–188
Steege DA, Söll DG (1979) Suppression. In: Goldberger RF (ed) Biological Regulation and Development (vol 1 ). Plenum, New York, pp 433–485
Stephens RM, Casey JW, Rice NR (1986) Equine infectious anemia virus gag and pot genes: relatedness to visna and AIDS virus. Science 231: 589–594
Stewart T, Sharp S (1984) Characterizing the function of Ofi-phosphoseryl-tRNA. Methods Enzymol 106: 157–161
Strauss EG, Rice CM, Strauss JH (1983) Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon. Proc Natl Acad Sci USA 80: 5271–5275
Strauss EG, Rice CM, Strauss JH (1984) Complete nucleotide sequence of the genomic RNA of Sindbis virus. Virology 133: 92–110
Sukenaga Y, Ishida K, Takeda T, Takagi K (1987) cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res 15: 71–78
Summers WP, Summers WC, Laski FA, RajBhandary UL, Sharp PA (1983) Functional suppression in mammalian cells of nonsense mutations in the Herpes simplex virus thymidine kinase gene by suppressor tRNA genes. J Virol 47: 376–379
Sundee RA, Evenson JK (1987) Serine incorporation into the selenocysteine moiety of glutathione peroxidase. J Biol Chem 262: 933–937
Suter B, Altwegg M, Choffat Y, Kubli E (1986) The nucleotide sequence of two homogeneic Drosophila melanogaster tRNATY isoacceptors: application of a rapid tRNA anticodon sequencing method using S-1 nuclease. Arch Biochem Biophys 247: 233–237
Temple GF, Dozy AM, Roy KL, Kan YW (1982) Construction of a functional human suppressor tRNA gene: an approach to gene therapy for beta-thalassaemia. Nature 296: 537–540
Thayer RM, Power MD, Bryant ML, Gardner MB, Barr PJ, Luciw PA (1987) Sequence relationships of type D retroviruses which cause simian acquired immunodeficiency syndrome. Virology 157: 317–329
Topai MD, Fresco JR (1976) Complementary base pairing and the origin of substitution mutations. Nature 263: 285–289
Tukalo MA, Vlasov V, Vasil’chenko I, Matsuka G, Knorre D (1980) Dokl Akad Nauk SSSR 253: 253–256
Valle RPC, Morch M-D (1988) Stop making sense or regulation at the level of termination in eukaryotic protein synthesis. FEBS Lett 235: 1–15
Valle RPC, Morch M-D, Haenni A-L (1987) Novel amber suppressor tRNAs of mammalian origin. EMBO J 6: 3049–3055
Vasil’ieva IG, Tukalo MA, Krikliviy IA, Matduka GCH (1984) Mol Biol Akad Nauk SSSR 18: 1321–1325
Wain-Hobson S, Sonigo P, Danos O, Cole S, Alizon M (1985) Nucleotide sequence of the AIDS virus, LAV. Cell 40: 9–17
Ward DC, Reich E (1968) Conformational properties of polyformycin: a polyribonucleotide with individual residues in the syn conformation. Proc Natl Acad Sci USA 61: 1494–1501
Weiss WA, Friedberg EC (1986) Normal yeast tRNAG’n/CAG can suppress amber codons and is encoded by an essential gene. J Mol Biol 192: 725–735
Weiss RB, Dunn JF, Atkins JF, Gesteland RF (1987a) Slippery runs, shifty stops, backward steps, and forward hops:–2,–1, + 1, + 2, + 5, and + 6 ribosomal frameshifting. Cold Spring Harbor Symposia on Quantitative Biology vol II, Gold Spring Harbor, New York, pp 687–696
Weiss WA, Edelman I, Culbertson MR, Friedberg EC (1987b) Physiological levels of normal tRNA/CAG can effect partial suppression of amber mutations in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci USA 84: 8031–8034
Weiss R, Lindsley D, Falahee B, Gallant J (1988) On the mechanism of ribosomal frameshifting at hungry codons. J Mol Biol 203: 403–410
Wilson W, Braddock M, Adams S, Rathjen P, Kingsman S, Kingsman A (1988) HIV expression strategies: ribosomal frameshifting is directed by a short sequence in both mammalian and yeast systems. Cell 55: 1159–1169
Yoshinaka Y, Katosh I, Copeland TD, Oroszlan S (1985a) Murine leukemia virus protease is encoded by the gag-pol gene and is synthesized through suppression of an amber termination codon. Proc Natl Acad Sci USA 82: 1618–1622
Yoshinaka Y, Katoh I, Copeland TD, Oroszlan S (1985b) Translational readthrough of an amber termination codon during synthesis of feline leukemia virus protease. J Virol 55: 870–873
Young JF, Capecchi M, Laski FA, RajBhandary UL, Sharp PA, Palese P (1983) Measurement of suppressor transfer RNA activity. Science 221: 873–875
Ziegler V, Richards K, Guilley H, Jonard T, Putz C (1985) Cell-free translation of beet necrotic yellow vein virus: readthrough of the coat protein cistron. J Gen Virol 66: 2079–2087
Zinoni F, Birkmann A, Leinfelder E, Böck A (1987) Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon. Proc Natl Acad Sci USA 84: 3156–3160
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Hatfield, D., Lee, B.J., Smith, D.W.E., Oroszlan, S. (1990). Role of Nonsense, Frameshift, and Missense Suppressor tRNAs in Mammalian Cells. In: Jeanteur, P., Kuchino, Y., Müller, W.E.G., Paine, P.L. (eds) Progress in Molecular and Subcellular Biology. Progress in Molecular and Subcellular Biology, vol 11. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75178-3_5
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