Skip to main content
NCBI home page
Elsevier - PMC COVID-19 Collection logoLink to Elsevier - PMC COVID-19 Collection
. 2004 Apr 30;62(3):413–423. doi: 10.1016/0092-8674(90)90007-2

Ribosome gymnastics—Degree of difficulty 9.5, style 10.0

John F Atkins ★,†, Robert B Weiss ★, Raymond F Gesteland ★
PMCID: PMC7133308  PMID: 2199062

The content is available as a PDF (1.4 MB).

References

  1. Atkins J.F., Elseviers D., Gorini L. Vol. 69. 1972. Low activity of β-galactosidase in frameshift mutants of Escherichia coli; pp. 1192–1195. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Atkins J.F., Gesteland R.F., Reid B.R., Anderson C.W. Normal tRNAs promote ribosomal frameshifting. Cell. 1979;18:1119–1131. doi: 10.1016/0092-8674(79)90225-3. [DOI] [PubMed] [Google Scholar]
  3. Atkins J.F., Nichols B.P., Thompson S. The nucleotide sequence of the first externally suppressible −1 frameshift mutant, and of some nearby leaky frameshift mutants. EMBO J. 1983;2:1345–1350. doi: 10.1002/j.1460-2075.1983.tb01590.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Belcourt M.F., Farabaugh P.J. Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce slippage on a 7 nucleotide minimal site. Cell. 1990;62 doi: 10.1016/0092-8674(90)90371-K. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Belland R.J., Morrison S.G., van der Ley P., Swanson J. Expression and phase variation of gonococcal P.II genes in Escherichia coli involves ribosomal frameshifting and slipped-strand mispairing. Mol. Microbiol. 1989;3:777–786. doi: 10.1111/j.1365-2958.1989.tb00226.x. [DOI] [PubMed] [Google Scholar]
  6. Beremand M.N., Blumenthal T. Overlapping genes in RNA phage: a new protein implicated in lysis. Cell. 1979;18:257–266. doi: 10.1016/0092-8674(79)90045-x. [DOI] [PubMed] [Google Scholar]
  7. Berkhout B., Schmidt B.F., van Strien A., van Boom J., van Westrenen J., van Duin J. Lysis gene of bacteriophage MS2 is activated by translation termination of the overlapping coat gene. J. Mol. Biol. 1987;195:517–524. doi: 10.1016/0022-2836(87)90180-x. [DOI] [PubMed] [Google Scholar]
  8. Blinkowa A.L., Walker J.R. Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III γ subunit from within the τ subunit reading frame. Nucl. Acids Res. 1990;18:1725–1729. doi: 10.1093/nar/18.7.1725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Böck A., Stadtman T. Selenocysteine, a highly specific component of certain enzymes, is incorporated by a UGA-directed co-translational mechanism. BioFactors. 1988;1:245–250. [PubMed] [Google Scholar]
  10. Bredenbeek P.J., Pachuk C.J., Noten A.F.H., Charité J., Luytjes W., Weiss S.R., Spaan W.J.M. The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism. Nucl. Acids Res. 1990;18:1825–1832. doi: 10.1093/nar/18.7.1825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Brierley I., Boursnell M.E.G., Binns M.M., Bilimoria B., Blok V.C., Brown T.D.K., Inglis S.C. An efficient ribosomal frameshifting signal in the polymerase-encoding region of the coronavirus IBV. EMBO J. 1987;6:3779–3785. doi: 10.1002/j.1460-2075.1987.tb02713.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Brierley I., Digard P., Inglis S.C. Characterization of an efficient coronavirus ribosomal frameshifting signal: requirement for an RNA pseudoknot. Cell. 1989;57:537–547. doi: 10.1016/0092-8674(89)90124-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Bruce A.G., Atkins J.F., Gesteland R.F. Vol. 83. 1986. tRNA anticodon replacement experiments show that ribosomal frameshifting can be caused by doublet decoding; pp. 5062–5066. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Buckley K.J., Hayashi M. Role of premature translational termination in the regulation of expression of the ϕX174 lysis gene. J. Mol. Biol. 1987;198:599–607. doi: 10.1016/0022-2836(87)90203-8. [DOI] [PubMed] [Google Scholar]
  15. Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., Harrison P.R. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the “termination” codon, TGA. EMBO J. 1986;5:1221–1227. doi: 10.1002/j.1460-2075.1986.tb04350.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Chang L.-J., Pryciak P., Ganem D., Varmus H.E. Biosynthesis of the reverse transcriptase of hepatitis B viruses involves de novo translational initiation not ribosomal frameshifting. Nature. 1989;337:364–368. doi: 10.1038/337364a0. [DOI] [PubMed] [Google Scholar]
  17. Clare J., Farabaugh P. Vol. 82. 1985. Nucleotide sequence of a yeast Ty element: evidence for an unusual mechanism of gene expression; pp. 2829–2833. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Craigen W.J., Cook R.G., Tate W.P., Caskey C.T. Vol. 82. 1985. Bacterial peptide chain release factors: conserved primary structure and possible frameshift regulation of release factor 2; pp. 3616–3620. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Crick F.H.C., Brenner S., Klug A., Pieczenik G. A speculation on the origin of protein synthesis. Origins of Life. 1976;7:389–397. doi: 10.1007/BF00927934. [DOI] [PubMed] [Google Scholar]
  20. Culbertson M.R., Leeds P., Sandbaken M.G., Wilson P.G. Frameshift suppression. In: Hill W., Moore P., Garrett R., Warner J., Dahlberg A., Schlessinger D., editors. Ribosomes: Structure and Function. American Society for Microbiology; Washington, D.C.,: 1990. in press. [Google Scholar]
  21. Curran J.F., Yarus M. Use of tRNA suppressors to probe regulation of Escherichia coli release factor 2. J. Mol. Biol. 1988;203:75–83. doi: 10.1016/0022-2836(88)90092-7. [DOI] [PubMed] [Google Scholar]
  22. Dahlberg A.E. The functional role of ribosomal RNA in protein synthesis. Cell. 1989;57:525–529. doi: 10.1016/0092-8674(89)90122-0. [DOI] [PubMed] [Google Scholar]
  23. Dayhuff T.J., Atkins J.F., Gesteland R.F. Characterization of ribosomal frameshift events by protein sequence analysis. J. Biol. Chem. 1986;261:7491–7500. [PubMed] [Google Scholar]
  24. Diamond A., Dudock B., Hatfield D. Structure and properties of a bovine liver UGA suppressor serine tRNA with a tryptophan anticodon. Cell. 1981;25:497–506. doi: 10.1016/0092-8674(81)90068-4. [DOI] [PubMed] [Google Scholar]
  25. Diamond M.E., Dowhanick J.J., Nemeroff M.E., Pietras D.F., Tu C., Bruenn J.A. Overlapping genes in a yeast double-stranded RNA virus. J. Virol. 1989;63:3983–3990. doi: 10.1128/jvi.63.9.3983-3990.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Dunn J.J., Studier F.W. Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J. Mol. Biol. 1983;166:477–535. doi: 10.1016/s0022-2836(83)80282-4. [DOI] [PubMed] [Google Scholar]
  27. Falahee M.B., Weiss R.B., O'Connor M., Doonan S., Gesteland R.F., Atkins J.F. Mutants of translational components that alter reading frame by two steps forward or one step back. J. Biol. Chem. 1988;263:18099–18103. [PubMed] [Google Scholar]
  28. Felsenstein K.M., Goff S.P. Expression of the gag-pol fusion protein of Moloney murine leukemia virus without gag protein does not induce virion formation or proteolytic processing. J. Virol. 1988;62:2179–2182. doi: 10.1128/jvi.62.6.2179-2182.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Feng Y.-X., Levin J.G., Hatfield D.L., Schaefer T.S., Gorelick R.J., Rein A. Suppression of UAA and UGA termination codons in mutant murine leukemia viruses. J. Virol. 1989;63:2870–2873. doi: 10.1128/jvi.63.6.2870-2873.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Feng Y.-X., Hatfield D.L., Rein A., Levin J.G. Translational readthrough of the murine leukemia virus gag gene amber codon does not require virus-induced alteration of tRNA. J. Virol. 1989;63:2405–2410. doi: 10.1128/jvi.63.5.2405-2410.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Flower A.M., McHenry C.S. Vol. 87. 1990. The γ subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting; pp. 3713–3717. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Forchhammer K., Rücknagel K.-P., Böck A. Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis. J. Biol. Chem. 1990;265:9346–9350. [PubMed] [Google Scholar]
  33. Fox T.D., Weiss-Brummer B. Leaky +1 and −1 frameshift mutations at the same site in a yeast mitochondrial gene. Nature. 1980;288:60–63. doi: 10.1038/288060a0. [DOI] [PubMed] [Google Scholar]
  34. Gollnick P., Yanofsky C. tRNATrp translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon. J. Bacteriol. 1990;172:3100–3107. doi: 10.1128/jb.172.6.3100-3107.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Hansen L.J., Chalker D.L., Sandmeyer S.B. Ty3, a yeast retrotransposon associated with tRNA genes, has homology to animal retroviruses. Mol. Cell. Biol. 1988;8:5245–5256. doi: 10.1128/mcb.8.12.5245. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Hatfield D., Feng Y.-X., Lee B.J., Rein A., Levin J.G., Oroszlan S. Chromatographic analysis of the aminoacyl-tRNAs which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV. Virology. 1989;173:736–742. doi: 10.1016/0042-6822(89)90589-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Hizi A., Henderson L.E., Copeland T.D., Sowder R.C., Hixson C.V., Oroszlan S. Vol. 84. 1987. Characterization of mouse mammary tumor virus gag-pro gene products and the ribosomal frameshift site by protein sequencing; pp. 7041–7045. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Hofstetter H., Monstein H.-J., Weissman C. The readthrough protein A1 is essential for the formation of viable Qβ particles. Biochim. Biophys. Acta. 1974;374:238–251. doi: 10.1016/0005-2787(74)90366-9. [DOI] [PubMed] [Google Scholar]
  39. Huang W.M., Ao S.-Z., Casjens S., Orlandi R., Zeikus R., Weiss R., Winge D., Fang M. A persistent untranslated sequence within bacteriophage T4 DNA topoisomerase gene 60. Science. 1988;239:1005–1012. doi: 10.1126/science.2830666. [DOI] [PubMed] [Google Scholar]
  40. Hughes D., Thompson S., O'Connor M., Tuohy T., Nichols B.P., Atkins J.F. Genetic characterization of frameshift suppressors with new decoding properties. J. Bacteriol. 1989;171:1028–1034. doi: 10.1128/jb.171.2.1028-1034.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Icho T., Wickner R.B. The double-stranded RNA genome of yeast virus L-A encodes its own putative RNA polymerase by fusing two open reading frames. J. Biol. Chem. 1989;264:6716–6723. [PubMed] [Google Scholar]
  42. Ishikawa M., Meshi T., Motoyoshi F., Takamatsu N., Okada Y. In vitro mutagenesis of the putative replicase genes of tobacco mosaic virus. Nucl. Acids Res. 1986;14:8291–8305. doi: 10.1093/nar/14.21.8291. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Jacks T., Varmus H.E. Expression of the Rous sarcoma virus pol gene by ribosomal frameshifting. Science. 1985;230:1237–1242. doi: 10.1126/science.2416054. [DOI] [PubMed] [Google Scholar]
  44. Jacks T., Townsley K., Varmus H.E., Majors J. Vol. 84. 1987. Two efficient ribosomal frameshifting events are required for synthesis of mouse mammary tumor virus gag-related polyproteins; pp. 4298–4302. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Jacks T., Madhani H.D., Masiarz F.R., Varmus H.E. Signals for ribosomal frameshifting in the Rous sarcoma virus gag-pol region. Cell. 1988;55:447–458. doi: 10.1016/0092-8674(88)90031-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Jacks T., Power M.D., Masiarz F.R., Luciw P.A., Barr P.J., Varmus H.E. Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature. 1988;331:280–283. doi: 10.1038/331280a0. [DOI] [PubMed] [Google Scholar]
  47. Jalajakumari M.B., Thomas C.J., Halter R., Manning P.A. Genes for biosynthesis and assembly of CS3 pili of CFA/II enterotoxigenic Escherichia coli: novel regulation of pilus production by bypassing an amber codon. Mol. Microbiol. 1989;3:1685–1695. doi: 10.1111/j.1365-2958.1989.tb00154.x. [DOI] [PubMed] [Google Scholar]
  48. Jones D.S., Nemoto F., Kuchino Y., Masuda M., Yoshikura H., Nishimura S. The effect of specific mutations at and around the gag-pol gene junction of Moloney murine leukaemia virus. Nucl. Acids Res. 1989;15:5933–5945. doi: 10.1093/nar/17.15.5933. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Kastelein R.A., Remaut E., Fiers W., van Duin J. Lysis gene expression of RNA phage MS2 depends on a frameshift during translation of the overlapping coat protein gene. Nature. 1982;295:35–41. doi: 10.1038/295035a0. [DOI] [PubMed] [Google Scholar]
  50. Kikuchi Y., Shimatake H., Kikuchi A. A yeast gene required for the G1-to-S transition encodes a protein containing an A-kinase target site and GTPase domain. EMBO J. 1988;7:1175–1182. doi: 10.1002/j.1460-2075.1988.tb02928.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Kuchino Y., Beier H., Akita N., Nishimura S. Vol. 84. 1987. Natural UAG suppressor glutamine tRNA is elevated in mouse cells infected with Moloney murine leukemia virus; pp. 2668–2672. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Kuchino Y., Nishimura S., Schröder H.C., Rottmann M., Müller W.E.G. Selective inhibition of formation of suppressor glutamine tRNA in Moloney murine leukemia virus-infected NIH-3T3 cells by avarol. Virology. 1988;65:518–526. doi: 10.1016/0042-6822(88)90596-x. [DOI] [PubMed] [Google Scholar]
  53. Kurland C.G. Reading frame errors on ribosomes. In: Celis J.E., Smith J.D., editors. Nonsense Mutations and tRNA Suppressors. Academic Press; New York: 1979. pp. 97–108. [Google Scholar]
  54. Le S.-Y., Chen J.-H., Maizel J.V. Thermodynamic stability and statistical significance of potential stem-loop structures situated at the frameshift sites of retroviruses. Nucl. Acids Res. 1989;17:6143–6152. doi: 10.1093/nar/17.15.6143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Lee B.J., Worland P.J., Davis J.N., Stadtman T.C., Hatfield D.L. Identification of a selenocysteyl-tRNASer in mammalian cells that recognizes the nonsense codon, UGA. J. Biol. Chem. 1989;264:9724–9727. [PubMed] [Google Scholar]
  56. Leinfelder W., Forchhammer K., Veprek B., Zehelein E., Böck A. Vol. 87. 1990. In vitro synthesis of selenocysteinyl-tRNAUCA from seryl-tRNAUCA: involvement and characterization of the selD gene product; pp. 543–547. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Li G., Rice C. Mutagenesis of the in-frame opal termination codon preceding nsP4 of sindbis virus: studies of translational readthrough and its effect on virus replication. J. Virol. 1989;63:1326–1337. doi: 10.1128/jvi.63.3.1326-1337.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Mellor J., Fulton S.M., Dobson M.J., Wilson W., Kingsman S.M., Kingsman A.J. A retrovirus-like strategy for expression of a fusion protein encoded by yeast transposon Ty1. Nature. 1985;313:243–246. doi: 10.1038/313243a0. [DOI] [PubMed] [Google Scholar]
  59. Miller W.A., Waterhouse P.M., Gerlach W.L. Sequence and organization of barley yellow dwarf virus genomic RNA. Nucl. Acids Res. 1988;16:6097–6111. doi: 10.1093/nar/16.13.6097. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Moazed D., Noller H.F. Intermediate states in the movement of transfer RNA in the ribosome. Nature. 1989;342:142–148. doi: 10.1038/342142a0. [DOI] [PubMed] [Google Scholar]
  61. Moore R., Dixon M., Smith R., Peters G., Dickson C. Complete nucleotide sequence of a milk-transmitted mouse mammary tumor virus: two frameshift events are required for translation of gag and pol. J. Virol. 1987;61:480–490. doi: 10.1128/jvi.61.2.480-490.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Noller H.F., Asire M., Barta A., Douthwaite S., Goldstein T., Gutell R.R., Moazed D., Normanly J., Prince J.B., Stern S., Triman K., Turner S., VanStolk B., Wheaton V., Weiser B., Woese C.R. Studies on the structure and function of ribosomal RNA. In: Hardesty B., Kramer G., editors. Structure, Function and Genetics of Ribosomes. Springer-Verlag; New York: 1986. pp. 143–163. [Google Scholar]
  63. Nutter R.C., Scheets K., Panganiban L.C., Lommel S.A. The complete nucleotide sequence of the maize chlorotic mottle virus genome. Nucl. Acids Res. 1989;17:3163–3177. doi: 10.1093/nar/17.8.3163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. O'Connor M., Gesteland R.F., Atkins J.F. tRNA hopping: enhancement by an expanded anticodon. EMBO J. 1989;8:4315–4323. doi: 10.1002/j.1460-2075.1989.tb08618.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. O'Mahony D.J., Mims B.H., Thompson S., Murgola E.J., Atkins J.F. Vol. 86. 1989. Glycine tRNA mutants with normal anticodon loop size cause −1 frameshifting; pp. 7979–7983. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Panganiban A.T. Retroviral gag gene amber codon suppression is caused by an intrinsic cis-acting component of the viral mRNA. J. Virol. 1988;62:3574–3580. doi: 10.1128/jvi.62.10.3574-3580.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Pelham H.R.B. Leaky UAG termination codon in tobacco mosaic virus RNA. Nature. 1978;272:469–471. doi: 10.1038/272469a0. [DOI] [PubMed] [Google Scholar]
  68. Philipson L., Andersson P., Olshevsky U., Weinberg R., Baltimore D., Gesteland R. Translation of MuLV and MSV RNAs in nuclease-treated reticulocyte extracts: enhancement of the gag-pol polypeptide with yeast suppressor tRNA. Cell. 1978;13:189–199. doi: 10.1016/0092-8674(78)90149-6. [DOI] [PubMed] [Google Scholar]
  69. Prère M.-F., Chandler M., Fayet O. Transposition in Shigella: isolation and analysis of IS911, a new member of the IS3 group of insertion sequences. J. Bacteriol. 1990;172:4090–4099. doi: 10.1128/jb.172.7.4090-4099.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Rheinberger H.-J., Nierhaus K.H. Allosteric interactions between the ribosomal transfer RNA-binding sites A and E. J. Biol. Chem. 1986;261:9133–9139. [PubMed] [Google Scholar]
  71. Riddle D.L., Carbon J.C. Frameshift suppression: a nucleotide addition in the anticodon of a glycine transfer RNA. Nature New Biol. 1973;242:230–234. doi: 10.1038/newbio242230a0. [DOI] [PubMed] [Google Scholar]
  72. Riyasaty S., Atkins J.F. External suppression of a frameshift mutant in Salmonella. J. Mol. Biol. 1968;34:541–557. doi: 10.1016/0022-2836(68)90179-4. [DOI] [PubMed] [Google Scholar]
  73. 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. Nucl. Acids Res. 1989;17:7159–7165. doi: 10.1093/nar/17.18.7159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Schultze M., Hohn T., Jiricny J. The reverse transcriptase gene of cauliflower mosaic virus is translated separately from the capsid gene. EMBO J. 1990;9:1177–1185. doi: 10.1002/j.1460-2075.1990.tb08225.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Sekine Y., Ohtsubo E. Vol. 86. 1989. Frameshifting is required for production of the transposase encoded by, insertion sequence 1; pp. 4609–4613. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Spanjaard R.A., van Duin J. Vol. 85. 1988. Translation of the sequence AGG-AGG yields 50% ribosomal frameshift; pp. 7967–7971. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Spirin A.S. Structural dynamic aspects of protein synthesis on ribosomes. Biochimie. 1987;69:949–956. doi: 10.1016/0300-9084(87)90228-8. [DOI] [PubMed] [Google Scholar]
  78. Strauss E.G., Rice C.M., Strauss J.H. Vol. 80. 1983. Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon; pp. 5271–5275. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Takkinen K. Complete nucleotide sequence of the nonstructural protein genes of Semliki Forest virus. Nucl. Acids Res. 1986;14:5667–5682. doi: 10.1093/nar/14.14.5667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. ten Dam E.B., Pleij C.W.A., Bosch L. RNA pseudoknots: translational frameshifting and readthrough on viral RNAs. Virus Genes. 1990;4 doi: 10.1007/BF00678404. in press. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Trifonov E.N. Translation framing code and frame-monitoring mechanism as suggested by the analysis of mRNA and 16S rRNA nucleotide sequences. J. Mol. Biol. 1987;194:643–652. doi: 10.1016/0022-2836(87)90241-5. [DOI] [PubMed] [Google Scholar]
  82. Tsuchihashi Z., Kornberg A. Vol. 87. 1990. Translational frameshifting generates the γ subunit of DNA polymerase III holoenzyme; pp. 2516–2520. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Tuohy T.M.F., Thompson S., Hughes D., Gesteland R.F., Atkins J.F. The role of EF-Tu and other translation components in determining translocation step size. Biochim. Biophys. Acta. 1990 doi: 10.1016/0167-4781(90)90180-a. in press. [DOI] [PubMed] [Google Scholar]
  84. Veidt I., Lot H., Leiser M., Scheidecker D., Guilley H., Richards K., Jonard G. Nucleotide sequence of beet western yellows virus RNA. Nucl. Acids Res. 1988;16:9917–9932. doi: 10.1093/nar/16.21.9917. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Waters A.P., Syin C., McCutchan T.F. Developmental regulation of stage-specific ribosome populations in Plasmodium. Nature. 1989;342:438–440. doi: 10.1038/342438a0. [DOI] [PubMed] [Google Scholar]
  86. Weiner A.M., Weber K. A single UGA codon functions as a natural termination signal in the coliphage Qβ coat protein cistron. J. Mol. Biol. 1973;80:837–855. doi: 10.1016/0022-2836(73)90213-1. [DOI] [PubMed] [Google Scholar]
  87. Weiss R.B. Vol. 81. 1984. Molecular model of ribosome frameshifting; pp. 5797–5801. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Weiss R.B., Gallant J. Mechanism of ribosomal frameshifting during translation of the genetic code. Nature. 1983;302:389–393. doi: 10.1038/302389a0. [DOI] [PubMed] [Google Scholar]
  89. Weiss R.B., Dunn D.M., Atkins J.F., Gesteland R.F. Vol. 52. 1987. Slippery runs, shifty stops, backward steps, and forward hops: −2, −1, +1, +2, +5, and +6 ribosomal frameshifting; pp. 687–693. (Cold Spring Harbor Symp. Quant. Biol.). [DOI] [PubMed] [Google Scholar]
  90. Weiss R.B., Dunn D.M., Dahlberg A.E., Atkins J.F., Gesteland R.F. Reading frame switch caused by base-pair formation between the 3′ end of 16S rRNA and the mRNA during elongation of protein synthesis in Escherichia coli. EMBO J. 1988;7:1503–1507. doi: 10.1002/j.1460-2075.1988.tb02969.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Weiss R.B., Lindsley D., Falahee B., Gallant J. On the mechanism of ribosomal frameshifting at hungry codons. J. Mol. Biol. 1988;203:403–410. doi: 10.1016/0022-2836(88)90008-3. [DOI] [PubMed] [Google Scholar]
  92. Weiss R.B., Dunn D.M., Shuh M., Atkins J.F., Gesteland R.F. E. coli ribosomes re-phase on retroviral frameshift signals at rates ranging from 2 to 50 percent. New Biol. 1989;1:159–169. [PubMed] [Google Scholar]
  93. Weiss R.B., Huang W.M., Dunn D.M. A nascent peptide is required for ribosomal bypass of the coding gap in bacteriophage T4 gene 60. Cell. 1990;62:117–126. doi: 10.1016/0092-8674(90)90245-A. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Weiss R.B., Dunn D.M., Atkins J.F., Gesteland R.F. Ribosomal frameshifting from −2 to +50 nucleotides. Prog. Nucl. Acids Res. Mol. Biol. 1990;39:159–183. doi: 10.1016/s0079-6603(08)60626-1. [DOI] [PubMed] [Google Scholar]
  95. Werner M., Feller A., Messenguy F., Piérard A. The leader peptide of yeast gene CPA1 is essential for the translational repression of its expression. Cell. 1987;49:805–813. doi: 10.1016/0092-8674(87)90618-0. [DOI] [PubMed] [Google Scholar]
  96. Whitfield H.J., Martin R.G., Ames B.N. Classification of aminotransferase (C gene) mutants in the histidine operon. J. Mol. Biol. 1966;21:335–355. doi: 10.1016/0022-2836(66)90103-3. [DOI] [PubMed] [Google Scholar]
  97. Wilson P.G., Culbertson M.R. suf12 suppressor protein of yeast. A fusion protein related to the EF-1 family of elongation factorsJ. Mol. Biol. 1988;199:559–573. doi: 10.1016/0022-2836(88)90301-4. [DOI] [PubMed] [Google Scholar]
  98. Wilson W., Braddock M., Adams S.E., Rathjen P.D., Kingsman S.M., Kingsman A.J. HIV expression strategies: ribosomal frameshifting is directed by a short sequence in both mammalian and yeast systems. Cell. 1988;55:1159–1169. doi: 10.1016/0092-8674(88)90260-7. [DOI] [PubMed] [Google Scholar]
  99. Witte O.N., Baltimore D. Relationship of retrovirus polyprotein cleavages to virion maturation studied with temperature-sensitive murine leukemia virus mutants. J. Virol. 1978;26:750–761. doi: 10.1128/jvi.26.3.750-761.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  100. Woese C. Molecular mechanics of translation: a reciprocating ratchet mechanism. Nature. 1970;226:817–820. doi: 10.1038/226817a0. [DOI] [PubMed] [Google Scholar]
  101. Wolin S.L., Walter P. Ribosome pausing and stacking during translation of a eukaryotic mRNA. EMBO J. 1988;7:3559–3569. doi: 10.1002/j.1460-2075.1988.tb03233.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Wong S.C., Abdelal A.T. Unorthodox expression of an enzyme: evidence for an untranslated region within carA from Pseudomonas aeruginosa. J. Bacteriol. 1990;172:630–642. doi: 10.1128/jb.172.2.630-642.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Xiong Z., Lommel S.A. The complete nucleotide sequence and genome organization of red clover necrotic mosaic virus RNA-1. Virology. 1989;171:543–554. doi: 10.1016/0042-6822(89)90624-7. [DOI] [PubMed] [Google Scholar]
  104. Xu H., Boeke J.D. Vol. 87. 1990. Inhibition of Ty1 transposition by mating pheromone in yeast. (Proc. Natl. Acad. Sci. USA). in press. [Google Scholar]
  105. Yen T.J., Machlin P.S., Cleveland D.W. Autoregulated instability of β-tubulin mRNAs by recognition of the nascent amino terminus of β-tubulin. Nature. 1988;334:580–585. doi: 10.1038/334580a0. [DOI] [PubMed] [Google Scholar]
  106. Yoshinaka Y., Katoh I., Copeland T.D., Oroszlan S. Vol. 82. 1985. Murine leukemia virus protease is encoded by the gag-pol gene and is synthesized through suppression of an amber termination codon; pp. 1618–1622. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Yoshinaka Y., Katoh I., Copeland T.D., Oroszlan S. Translational readthrough of an amber termination codon during synthesis of feline leukemia virus protease. J. Virol. 1985;55:870–873. doi: 10.1128/jvi.55.3.870-873.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Zinoni F., Birkmann A., Stadtman T.C., Böck A. Vol. 83. 1986. Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli; pp. 4650–4654. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Zinoni F., Heider J., Böck A. Vol. 87. 1990. Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine; pp. 4660–4664. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Cell are provided here courtesy of Elsevier

RESOURCES