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Effect of zinc ions on tRNA structure: imino proton NMR spectroscopy

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00415a057· OSTI ID:7187481

The structure of tRNA in solution was explored by NMR spectroscopy to evaluate the effect of divalent cations, especially zinc, which has a profound effect on the chromatographic behavior of tRNAs in certain systems. The divalent ions Mg/sup 2 +/ and Zn/sup 2 +/ have specific effects on the imino proton region of the /sup 1/H NMR spectrum of valine transfer RNA (tRNA/sup Val/) of Escherichia coli and of phenylalanine transfer RNA (tRNA/sup Phe/) of yeast. The dependence of the imino proton spectra of the two tRNAs was examined as a function of Zn/sup 2 +/ concentration. In both tRNAs the tertiary base pair (G-15) x (C-48) was markedly affected by Zn/sup 2 +/ (shifted downfield possibly by as much as 0.4 ppm); this is the terminal base pair in the augmented dihydrouridine helix (D-helix). Base pair (U-8) x (A-14) in yeast tRNA/sup Phe/ or (s/sup 4/U-8) x (A-14) in tRNA/sub 1//sup Val/, which are stacked on (G-15) x (C-48), was not affected by Zn/sup 2 +/, except when 1-2 Mg/sup 2 +/ ions per tRNA were also present. Another imino proton that may be affected by Zn/sup 2 +/ in both tRNAs is that of the tertiary base pair (G-19) x (C-46). The assignment of this resonance in yeast tRNA/sup Phe/ is tentative since it is located in the region of highly overlapping resonances between 12.6 and 12.3 ppm. This base pair helps to anchor the D-loop to the T Psi C loop. Surprisingly, the imino proton of (G-18) x (Psi-55) is not similarly affected by Zn/sup 2 +/, indicating that the effect of Zn/sup 2 +/ is not on G-57 which is the central non-hydrogen-bonded base in the guanosine sandwich created by the stacking of G-19, G-57, and G-20. The solution structure of tRNA/sup Phe/ shows marked correlation to the crystal structure in terms of Zn/sup 2 +/ interactions.

Research Organization:
Oak Ridge National Lab., TN (USA)
DOE Contract Number:
AC05-84OR21400
OSTI ID:
7187481
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:15; ISSN BICHA
Country of Publication:
United States
Language:
English