High-resolution phosphorus nuclear magnetic resonance spectroscopy of transfer ribonucleic acids: multiple conformations in the anticodon loop - PubMed (original) (raw)
High-resolution phosphorus nuclear magnetic resonance spectroscopy of transfer ribonucleic acids: multiple conformations in the anticodon loop
D G Gorenstein et al. Biochemistry. 1982.
Abstract
The temperature dependence of the 31P NMR spectra of yeast phenylalanine tRNA, E. coli tyrosine, glutamate (2), and formylmethionine tRNA is presented. The major difference between the 31P NMR spectra of the different acceptor tRNAs is in the main cluster region between -0.5 and -1.3 ppm. This confirms an earlier assignment of the main cluster region to the undistorted phosphate diesters in the hairpin loops and helical stems. In addition the 31P NMR spectra for all tRNAs reveal approximately 16 nonhelical diester signals spread over approximately 7 ppm besides the downfield terminal 3'-phosphate monoester. In the presence of 10 mM Mg2+ most scattered and main cluster signals do not shift between 22 and 66 degrees C, thus supporting our earlier hypothesis that 31P chemical shifts are sensitive to phosphate ester torsional and bond angles. At greater than 70 degrees C, all of the signals merge into a single random-coil conformation signal. A number of the scattered peaks are shifted (0.2-1.7 ppm) and broadened between 22 and 66 degrees C in the presence of Mg2+ and spermine as a result of a conformational transition in the anticodon loop. The 31P NMR spectrum of the dimer formed between yeast tRNAPhe and E. coli tRNA 2Glu is reported. This dimer simulates codon-anticodon interaction since the anticodon triplets of the two tRNAs are complementary. Evidence is presented that the anticodon-anticodon interaction alters the anticodon conformation and partially disrupts the tertiary structure of the tRNA.
Similar articles
- High resolution phosphorus NMR spectroscopy of transfer ribonucleic acids.
Gorenstein DG, Goldfield EM. Gorenstein DG, et al. Mol Cell Biochem. 1982 Jul 23;46(2):97-120. doi: 10.1007/BF00236777. Mol Cell Biochem. 1982. PMID: 6180293 - Imino proton NMR assignments and ion-binding studies on Escherichia coli tRNA3Gly.
Hyde EI. Hyde EI. Eur J Biochem. 1986 Feb 17;155(1):57-68. doi: 10.1111/j.1432-1033.1986.tb09458.x. Eur J Biochem. 1986. PMID: 2419133 - High-resolution nuclear magnetic resonance investigations of the structure of tRNA in solution.
Kearns DR. Kearns DR. Prog Nucleic Acid Res Mol Biol. 1976;18:91-149. doi: 10.1016/s0079-6603(08)60587-5. Prog Nucleic Acid Res Mol Biol. 1976. PMID: 790475 Review. No abstract available. - Crystallization of transfer ribonucleic acids.
Dock AC, Lorber B, Moras D, Pixa G, Thierry JC, Giégé R. Dock AC, et al. Biochimie. 1984 Mar;66(3):179-201. doi: 10.1016/0300-9084(84)90063-4. Biochimie. 1984. PMID: 6204693 Review.
Cited by
- The uridine in "U-turn": contributions to tRNA-ribosomal binding.
Ashraf SS, Ansari G, Guenther R, Sochacka E, Malkiewicz A, Agris PF. Ashraf SS, et al. RNA. 1999 Apr;5(4):503-11. doi: 10.1017/s1355838299981931. RNA. 1999. PMID: 10199567 Free PMC article.