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. 1996 Oct 29;93(22):12078–12081. doi: 10.1073/pnas.93.22.12078

Interplay of tRNA-like structures from plant viral RNAs with partners of the translation and replication machineries.

R Giegé 1
PMCID: PMC37945  PMID: 8901535

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blumenthal T., Carmichael G. G. RNA replication: function and structure of Qbeta-replicase. Annu Rev Biochem. 1979;48:525–548. doi: 10.1146/annurev.bi.48.070179.002521. [DOI] [PubMed] [Google Scholar]
  2. David C., Gargouri-Bouzid R., Haenni A. L. RNA replication of plant viruses containing an RNA genome. Prog Nucleic Acid Res Mol Biol. 1992;42:157–227. doi: 10.1016/s0079-6603(08)60576-0. [DOI] [PubMed] [Google Scholar]
  3. Dreher T. W., Hall T. C. Mutational analysis of the sequence and structural requirements in brome mosaic virus RNA for minus strand promoter activity. J Mol Biol. 1988 May 5;201(1):31–40. doi: 10.1016/0022-2836(88)90436-6. [DOI] [PubMed] [Google Scholar]
  4. Dreher T. W., Rao A. L., Hall T. C. Replication in vivo of mutant brome mosaic virus RNAs defective in aminoacylation. J Mol Biol. 1989 Apr 5;206(3):425–438. doi: 10.1016/0022-2836(89)90491-9. [DOI] [PubMed] [Google Scholar]
  5. Dreher T. W., Tsai C. H., Florentz C., Giegé R. Specific valylation of turnip yellow mosaic virus RNA by wheat germ valyl-tRNA synthetase determined by three anticodon loop nucleotides. Biochemistry. 1992 Sep 29;31(38):9183–9189. doi: 10.1021/bi00153a010. [DOI] [PubMed] [Google Scholar]
  6. Dreher T. W., Tsai C. H., Skuzeski J. M. Aminoacylation identity switch of turnip yellow mosaic virus RNA from valine to methionine results in an infectious virus. Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12212–12216. doi: 10.1073/pnas.93.22.12212. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eriani G., Delarue M., Poch O., Gangloff J., Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990 Sep 13;347(6289):203–206. doi: 10.1038/347203a0. [DOI] [PubMed] [Google Scholar]
  8. Felden B., Florentz C., Giegé R., Westhof E. Solution structure of the 3'-end of brome mosaic virus genomic RNAs. Conformational mimicry with canonical tRNAs. J Mol Biol. 1994 Jan 14;235(2):508–531. doi: 10.1006/jmbi.1994.1010. [DOI] [PubMed] [Google Scholar]
  9. Giegé R., Puglisi J. D., Florentz C. tRNA structure and aminoacylation efficiency. Prog Nucleic Acid Res Mol Biol. 1993;45:129–206. doi: 10.1016/s0079-6603(08)60869-7. [DOI] [PubMed] [Google Scholar]
  10. Graffe M., Dondon J., Caillet J., Romby P., Ehresmann C., Ehresmann B., Springer M. The specificity of translational control switched with transfer RNA identity rules. Science. 1992 Feb 21;255(5047):994–996. doi: 10.1126/science.1372129. [DOI] [PubMed] [Google Scholar]
  11. Haenni A. L., Joshi S., Chapeville F. tRNA-like structures in the genomes of RNA viruses. Prog Nucleic Acid Res Mol Biol. 1982;27:85–104. doi: 10.1016/s0079-6603(08)60598-x. [DOI] [PubMed] [Google Scholar]
  12. Hall T. C. Transfer RNA-like structures in viral genomes. Int Rev Cytol. 1979;60:1–26. doi: 10.1016/s0074-7696(08)61257-7. [DOI] [PubMed] [Google Scholar]
  13. Hinchman S. K., Henikoff S., Schuster S. M. A relationship between asparagine synthetase A and aspartyl tRNA synthetase. J Biol Chem. 1992 Jan 5;267(1):144–149. [PubMed] [Google Scholar]
  14. Joshi R. L., Faulhammer H., Chapeville F., Sprinzl M., Haenni A. L. Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu. Nucleic Acids Res. 1984 Oct 11;12(19):7467–7478. doi: 10.1093/nar/12.19.7467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kern D., Giegé R., Ebel J. P. Incorrect aminoacylatins catalysed by the phenylalanyl-and valyl-tRNA synthetases from yeast. Eur J Biochem. 1972 Nov 21;31(1):148–155. doi: 10.1111/j.1432-1033.1972.tb02513.x. [DOI] [PubMed] [Google Scholar]
  16. Kohl R. J., Hall T. C. Aminoacylation of RNA from several viruses: amino acid specificity and differential activity of plant, yeast and bacterial synthetases. J Gen Virol. 1974 Nov;25(2):257–261. doi: 10.1099/0022-1317-25-2-257. [DOI] [PubMed] [Google Scholar]
  17. Kohl R. J., Hall T. C. Loss of infectivity of brome mosaic virus RNA after chemical modification of the 3' or 5' terminus. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2682–2686. doi: 10.1073/pnas.74.7.2682. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Litvak S., Tarragó A., Tarragó-Litvak L., Allende J. E. Elongation factor-viral genome interaction dependent on the aminoacylation of TYMV and TMV RNAs. Nat New Biol. 1973 Jan 17;241(107):88–90. doi: 10.1038/newbio241088a0. [DOI] [PubMed] [Google Scholar]
  19. Maizels N., Weiner A. M. Phylogeny from function: evidence from the molecular fossil record that tRNA originated in replication, not translation. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6729–6734. doi: 10.1073/pnas.91.15.6729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. McClain W. H. Rules that govern tRNA identity in protein synthesis. J Mol Biol. 1993 Nov 20;234(2):257–280. doi: 10.1006/jmbi.1993.1582. [DOI] [PubMed] [Google Scholar]
  21. Miller W. A., Bujarski J. J., Dreher T. W., Hall T. C. Minus-strand initiation by brome mosaic virus replicase within the 3' tRNA-like structure of native and modified RNA templates. J Mol Biol. 1986 Feb 20;187(4):537–546. doi: 10.1016/0022-2836(86)90332-3. [DOI] [PubMed] [Google Scholar]
  22. Nissen P., Kjeldgaard M., Thirup S., Polekhina G., Reshetnikova L., Clark B. F., Nyborg J. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science. 1995 Dec 1;270(5241):1464–1472. doi: 10.1126/science.270.5241.1464. [DOI] [PubMed] [Google Scholar]
  23. Oberg B., Philipson L. Binding of histidine to tobacco mosaic virus RNA. Biochem Biophys Res Commun. 1972 Aug 21;48(4):927–932. doi: 10.1016/0006-291x(72)90697-3. [DOI] [PubMed] [Google Scholar]
  24. Pinck M., Yot P., Chapeville F., Duranton H. M. Enzymatic binding of valine to the 3' end of TYMV-RNA. Nature. 1970 Jun 6;226(5249):954–956. doi: 10.1038/226954a0. [DOI] [PubMed] [Google Scholar]
  25. Pleij C. W. Pseudoknots: a new motif in the RNA game. Trends Biochem Sci. 1990 Apr;15(4):143–147. doi: 10.1016/0968-0004(90)90214-v. [DOI] [PubMed] [Google Scholar]
  26. Pulikowska J., Wojtaszek P., Korcz A., Michalski Z., Candresse T., Twardowski T. Immunochemical properties of elongation factors 1 of plant origin. Eur J Biochem. 1988 Jan 15;171(1-2):131–136. doi: 10.1111/j.1432-1033.1988.tb13768.x. [DOI] [PubMed] [Google Scholar]
  27. Rao A. L., Dreher T. W., Marsh L. E., Hall T. C. Telomeric function of the tRNA-like structure of brome mosaic virus RNA. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5335–5339. doi: 10.1073/pnas.86.14.5335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Rietveld K., Van Poelgeest R., Pleij C. W., Van Boom J. H., Bosch L. The tRNA-like structure at the 3' terminus of turnip yellow mosaic virus RNA. Differences and similarities with canonical tRNA. Nucleic Acids Res. 1982 Mar 25;10(6):1929–1946. doi: 10.1093/nar/10.6.1929. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Rudinger J., Florentz C., Giegé R. Histidylation by yeast HisRS of tRNA or tRNA-like structure relies on residues -1 and 73 but is dependent on the RNA context. Nucleic Acids Res. 1994 Nov 25;22(23):5031–5037. doi: 10.1093/nar/22.23.5031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Sablin E. P., Kull F. J., Cooke R., Vale R. D., Fletterick R. J. Crystal structure of the motor domain of the kinesin-related motor ncd. Nature. 1996 Apr 11;380(6574):555–559. doi: 10.1038/380555a0. [DOI] [PubMed] [Google Scholar]
  31. Saks M. E., Sampson J. R., Abelson J. N. The transfer RNA identity problem: a search for rules. Science. 1994 Jan 14;263(5144):191–197. doi: 10.1126/science.7506844. [DOI] [PubMed] [Google Scholar]
  32. Schimmel P., Giegé R., Moras D., Yokoyama S. An operational RNA code for amino acids and possible relationship to genetic code. Proc Natl Acad Sci U S A. 1993 Oct 1;90(19):8763–8768. doi: 10.1073/pnas.90.19.8763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Schimmel P. RNA pseudoknots that interact with components of the translation apparatus. Cell. 1989 Jul 14;58(1):9–12. doi: 10.1016/0092-8674(89)90395-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Schulman L. H., Pelka H. Anticodon switching changes the identity of methionine and valine transfer RNAs. Science. 1988 Nov 4;242(4879):765–768. doi: 10.1126/science.3055296. [DOI] [PubMed] [Google Scholar]
  35. Senger B., Despons L., Walter P., Fasiolo F. The anticodon triplet is not sufficient to confer methionine acceptance to a transfer RNA. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10768–10771. doi: 10.1073/pnas.89.22.10768. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Tsai C. H., Dreher T. W. Second-site suppressor mutations assist in studying the function of the 3' noncoding region of turnip yellow mosaic virus RNA. J Virol. 1992 Sep;66(9):5190–5199. doi: 10.1128/jvi.66.9.5190-5199.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Weiner A. M., Maizels N. tRNA-like structures tag the 3' ends of genomic RNA molecules for replication: implications for the origin of protein synthesis. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7383–7387. doi: 10.1073/pnas.84.21.7383. [DOI] [PMC free article] [PubMed] [Google Scholar]

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