Abstract
The association between Trp-tRNA and Pro-tRNA, which have complementary anticodon sequences, has been used as a probe of anticodon conformation. It is unaffected, however, by the base change in the D-stem present in UGA-suppressor Trp-tRNA. This does not support the hypothesis that UGA suppression depends upon a conformational change induced in the anticodon. The stable denatured form of wild-type Trp-tRNA no longer interacts with Pro-tRNA; the structure of the anticodon region must therefore be quite different in the denatured form.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Buckingham R. H., Danchin A. Fluorescence of tryptophanyl-tRNA(Trp) from E. coli; An interaction between the indole and tRNA and its dependence on tRNA conformation. FEBS Lett. 1973 Mar 1;30(2):236–238. doi: 10.1016/0014-5793(73)80659-3. [DOI] [PubMed] [Google Scholar]
- Buckingham R. H., Danchin A., Grunberg-Manago M. Denaturation of UGA suppressor tRNA-Trp from E. coli. Biochem Biophys Res Commun. 1974 Jan;56(1):1–8. doi: 10.1016/s0006-291x(74)80307-4. [DOI] [PubMed] [Google Scholar]
- Buckingham R. H., Danchin A., Grunberg-Manago M. The effect of an intramolecular cross-link on reversible denaturation in tryptophan transfer ribonucleic acid from Escherichia coli. Biochemistry. 1973 Dec 18;12(26):5393–5399. doi: 10.1021/bi00750a023. [DOI] [PubMed] [Google Scholar]
- Eisinger J., Blumberg W. E. Binding constants from zone transport of interacting molecules. Biochemistry. 1973 Sep 11;12(19):3648–3662. doi: 10.1021/bi00743a013. [DOI] [PubMed] [Google Scholar]
- Eisinger J. Complex formation between transfer RNA'S with complementary anticodons. Biochem Biophys Res Commun. 1971 May 21;43(4):854–861. doi: 10.1016/0006-291x(71)90695-4. [DOI] [PubMed] [Google Scholar]
- Favre A., Buchingham R., Thomas G. tRNA tertiary structure in solution as probed by the photochemically induced 8-13 cross-link. Nucleic Acids Res. 1975 Aug;2(8):1421–1431. doi: 10.1093/nar/2.8.1421. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gartland W. J., Sueoka N. Two interconvertible forms of tryptophanyl sRNA in E. coli. Proc Natl Acad Sci U S A. 1966 Apr;55(4):948–956. doi: 10.1073/pnas.55.4.948. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goodman H. M., Abelson J. N., Landy A., Zadrazil S., Smith J. D. The nucleotide sequences of tyrosine transfer RNAs of Escherichia coli. Eur J Biochem. 1970 Apr;13(3):461–483. doi: 10.1111/j.1432-1033.1970.tb00950.x. [DOI] [PubMed] [Google Scholar]
- Grosjean H., Takada C., Petre J. Complex formation between transfer RNAs with complementary anticodons: use of matrix bound tRNA. Biochem Biophys Res Commun. 1973 Aug 6;53(3):882–893. doi: 10.1016/0006-291x(73)90175-7. [DOI] [PubMed] [Google Scholar]
- Hall R. H. N6-(delta 2-isopentenyl)adenosine: chemical reactions, biosynthesis, metabolism, and significance to the structure and function of tRNA. Prog Nucleic Acid Res Mol Biol. 1970;10:57–86. doi: 10.1016/s0079-6603(08)60561-9. [DOI] [PubMed] [Google Scholar]
- Hirsh D., Gold L. Translation of the UGA triplet in vitro by tryptophan transfer RNA's. J Mol Biol. 1971 Jun 14;58(2):459–468. doi: 10.1016/0022-2836(71)90363-9. [DOI] [PubMed] [Google Scholar]
- Hirsh D. Tryptophan transfer RNA as the UGA suppressor. J Mol Biol. 1971 Jun 14;58(2):439–458. doi: 10.1016/0022-2836(71)90362-7. [DOI] [PubMed] [Google Scholar]
- Högenauer G. Binding of UGA to wild type and suppressor tryptophan tRNA from E. coli. FEBS Lett. 1974 Mar 1;39(3):310–312. doi: 10.1016/0014-5793(74)80137-7. [DOI] [PubMed] [Google Scholar]
- Ishida T., Sueoka N. Effect of ambient conditions on conformations of tryptophan transfer ribonucleic acid of Escherichia coli. J Biol Chem. 1968 Oct 25;243(20):5329–5336. [PubMed] [Google Scholar]
- Ishikura H., Yamada Y., Nishimura S. The nucleotide sequence of a serine tRNA from Escherichia coli. FEBS Lett. 1971 Jul 15;16(1):68–70. doi: 10.1016/0014-5793(71)80688-9. [DOI] [PubMed] [Google Scholar]
- Kurland C. G., Rigler R., Ehrenberg M., Blomberg C. Allosteric mechanism for codon-dependent tRNA selection on ribosomes. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4248–4251. doi: 10.1073/pnas.72.11.4248. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miller J. P., Hirst-Bruns M. E., Philipps G. R. Action of venom phosphodiesterase on transfer RNA from Escherichia coli. Biochim Biophys Acta. 1970 Sep 17;217(1):176–188. doi: 10.1016/0005-2787(70)90134-6. [DOI] [PubMed] [Google Scholar]
- Nishimura S., Harada F., Narushima U., Seno T. Purification of methionine-, valine-, phenylalanine- and tyrosine-specific tRNA from Escherichia coli. Biochim Biophys Acta. 1967 Jun 20;142(1):133–148. doi: 10.1016/0005-2787(67)90522-9. [DOI] [PubMed] [Google Scholar]
- Ofengand J. Assay for AA-tRNA recognition by the EFTu-GTP complex of Escherichia coli. Methods Enzymol. 1974;29:661–667. doi: 10.1016/0076-6879(74)29057-8. [DOI] [PubMed] [Google Scholar]
- Schwarz U., Lührmann R., Gassen H. G. On the mRNA induced conformational change of AA-tRNA exposing the T-pse-C-G sequence for binding to the 50S ribosomal subunit. Biochem Biophys Res Commun. 1974 Feb 4;56(3):807–814. doi: 10.1016/0006-291x(74)90677-9. [DOI] [PubMed] [Google Scholar]
- Strigini P., Brickman E. Analysis of specific misreading in Escherichia coli. J Mol Biol. 1973 Apr 25;75(4):659–672. doi: 10.1016/0022-2836(73)90299-4. [DOI] [PubMed] [Google Scholar]
- Takasaki Y., Imahori K. CD and fluorescence studies of tRNAPhe from baker's yeast. J Biochem. 1973 Sep;74(3):513–517. doi: 10.1093/oxfordjournals.jbchem.a130271. [DOI] [PubMed] [Google Scholar]
- Watanabe K., Imahori K. The conformation difference between tRNA Met f and formylmethionyl-tRNA Met f from E. coli. Biochem Biophys Res Commun. 1971 Oct 15;45(2):488–494. doi: 10.1016/0006-291x(71)90845-x. [DOI] [PubMed] [Google Scholar]