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. 1970 Jan;65(1):39–46. doi: 10.1073/pnas.65.1.39

Studies of Transfer RNA Tertiary Structure by Singlet-Singlet Energy Transfer*

Kenneth Beardsley 1,2,†, Charles R Cantor 1,2,‡
PMCID: PMC286187  PMID: 5263760

Abstract

This distance between a base next to the anticodon of tRNA and the 3′ CpCpA terminus of the molecule has been estimated by singlet-singlet energy transfer experiments. The energy donor was the Y base of unknown structure found in yeast tRNAphe. Three different energy acceptors were used: acriflavine, proflavinyl acetic acid hydrazide, and 9-hydrazino acridine. These were attached to the periodate-oxidized 3′ end of the tRNA. R0's between 24 and 30 Å were calculated for the three chromophore couples by assuming that the relative orientation of donor and acceptor is random. This assumption is supported by the consistency of the experimental results with all three acceptors and by studies of the fluorescence depolarization of Y. The energy transfer observed both by quenching of Y and enhanced activation of the acceptors is quite small, indicating that the anticodon is more than 40 Å away from the amino acid accepting terminus. This places severe restrictions on the type of tertiary structure possible for tRNA.

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Selected References

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

  1. Armstrong A., Hagopian H., Ingram V. M., Wagner E. K. Chemical studies on amino acid acceptor ribonucleic acids. VII. Partial ribonuclease digestion of alanine and valine soluble ribonucleic acid from yeast. Biochemistry. 1966 Sep;5(9):3027–3036. doi: 10.1021/bi00873a036. [DOI] [PubMed] [Google Scholar]
  2. CHURCHICH J. E. FLUORESCENCE STUDIES ON SOLUBLE RIBONUCLEIC ACID LABELLED WITH ACRIFLAVINE. Biochim Biophys Acta. 1963 Sep 24;75:274–276. doi: 10.1016/0006-3002(63)90608-5. [DOI] [PubMed] [Google Scholar]
  3. Cantor C. R., Jaskunas S. R., Tinoco I., Jr Optical properties of ribonucleic acids predicted from oligomers. J Mol Biol. 1966 Sep;20(1):39–62. doi: 10.1016/0022-2836(66)90116-1. [DOI] [PubMed] [Google Scholar]
  4. Cramer F., Doepner H., Haar F V. D., Schlimme E., Seidel H. On the conformation of transfer RNA. Proc Natl Acad Sci U S A. 1968 Dec;61(4):1384–1391. doi: 10.1073/pnas.61.4.1384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Haugland R. P., Yguerabide J., Stryer L. Dependence of the kinetics of singlet-singlet energy transfer on spectral overlap. Proc Natl Acad Sci U S A. 1969 May;63(1):23–30. doi: 10.1073/pnas.63.1.23. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Henley D. D., Lindahl T., Fresco J. R. Hydrodynamic changes accompanying the thermal denaturation of transfer ribonucleic acid. Proc Natl Acad Sci U S A. 1966 Jan;55(1):191–198. doi: 10.1073/pnas.55.1.191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. LATT S. A., CHEUNG H. T., BLOUT E. R. ENERGY TRANSFER. A SYSTEM WITH RELATIVELY FIXED DONOR-ACCEPTOR SEPARATION. J Am Chem Soc. 1965 Mar 5;87:995–1003. doi: 10.1021/ja01083a011. [DOI] [PubMed] [Google Scholar]
  8. Lake J. A., Beeman W. W. On the conformation of yeast transfer RNA. J Mol Biol. 1968 Jan 14;31(1):115–125. doi: 10.1016/0022-2836(68)90059-4. [DOI] [PubMed] [Google Scholar]
  9. Litt M. A simple procedure for the purification of yeast phenylalanine transfer RNA. Biochem Biophys Res Commun. 1968 Aug 13;32(3):507–511. doi: 10.1016/0006-291x(68)90691-8. [DOI] [PubMed] [Google Scholar]
  10. Litt M. Structural studies on transfer ribonucleic acid. I. Labeling of exposed guanine sites in yeast phenylalanine transfer ribonucleic acid with kethoxal. Biochemistry. 1969 Aug;8(8):3249–3253. doi: 10.1021/bi00836a017. [DOI] [PubMed] [Google Scholar]
  11. Madison J. T. Primary structure of RNA. Annu Rev Biochem. 1968;37:131–148. doi: 10.1146/annurev.bi.37.070168.001023. [DOI] [PubMed] [Google Scholar]
  12. Millar D. B., Steiner R. F. The effect of environment on the structure and helix-coil transition of soluble ribonucleic acid. Biochemistry. 1966 Jul;5(7):2289–2301. doi: 10.1021/bi00871a018. [DOI] [PubMed] [Google Scholar]
  13. Ninio J., Favre A., Yaniv M. Molecular model for transfer RNA. Nature. 1969 Sep 27;223(5213):1333–1335. doi: 10.1038/2231333a0. [DOI] [PubMed] [Google Scholar]
  14. Philipps G. R. Primary structure of transfer RNA. Nature. 1969 Jul 26;223(5204):374–377. doi: 10.1038/223374a0. [DOI] [PubMed] [Google Scholar]
  15. Stryer L. Fluorescence spectroscopy of proteins. Science. 1968 Nov 1;162(3853):526–533. doi: 10.1126/science.162.3853.526. [DOI] [PubMed] [Google Scholar]
  16. Stryer L., Haugland R. P. Energy transfer: a spectroscopic ruler. Proc Natl Acad Sci U S A. 1967 Aug;58(2):719–726. doi: 10.1073/pnas.58.2.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Thiebe R., Zachau H. G. A specific modification next to the anticodon of phenylalanine transfer ribonucleic acid. Eur J Biochem. 1968 Sep 24;5(4):546–555. doi: 10.1111/j.1432-1033.1968.tb00404.x. [DOI] [PubMed] [Google Scholar]
  18. Wimmer E., Maxwell I. H., Tener G. M. A simple method for isolating highly purified yeast phenylalanine transfer ribonucleic acid. Biochemistry. 1968 Jul;7(7):2623–2628. doi: 10.1021/bi00847a026. [DOI] [PubMed] [Google Scholar]
  19. Yaniv M., Favre A., Barrell B. G. Structure of transfer RNA. Evidence for interaction between two non-adjacent nucleotide residues in tRNA from Escherichia coli. Nature. 1969 Sep 27;223(5213):1331–1333. doi: 10.1038/2231331a0. [DOI] [PubMed] [Google Scholar]
  20. Yarus M., Berg P. Recognition of tRNA by isoleucyl-tRNA synthetase. Effect of substrates on the dynamics of tRNA-enzyme interaction. J Mol Biol. 1969 Jun 14;42(2):171–189. doi: 10.1016/0022-2836(69)90037-0. [DOI] [PubMed] [Google Scholar]
  21. Zamecnik P. C., Stephenson M. L., Scott J. F. PARTIAL PURIFICATION OF SOLUBLE RNA. Proc Natl Acad Sci U S A. 1960 Jun;46(6):811–822. doi: 10.1073/pnas.46.6.811. [DOI] [PMC free article] [PubMed] [Google Scholar]

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