High-resolution phosphorus nuclear magnetic resonance spectra of yeast phenylalanine transfer ribonucleic acid. Metal ion effects and tentative partial assignment of signals.
The temperature and metal ion dependence of the 31P NMR spectra of yeast phenylalanine tRNA is presented, and a tentative assignment of some of the individual phosphate signals is offered. Signals A, C, F, P, and T have been assigned to the magnesium binding site of phosphates by monitoring the magnesium ion dependence in the 31P NMR spectra. In the presence of 10 mM Mg2+, specific paramagnetic line broadening effects are observed for signals A, D, E, and U upon addition of 0.001-0.1 Mn2+ ion per tRNA molecule. Through the combination of the above metal in experiments, X-ray studies, and earlier 1H and 31P NMR studies [particularly the tRNA modification 31P NMR experiments of Salemink et al. [Salemink, P..J.M., Swarthof T., & Hilbers, C.W. (1979) Biochemistry 18, 3477]], an initial assignment of some of these signals is attempted.
D001483:Base Sequence; D008274:Magnesium; D009682:Magnetic Resonance Spectroscopy; D008345:Manganese; D009690:Nucleic Acid Conformation; D012346:RNA, Transfer, Amino Acyl; D012441:Saccharomyces cerevisiae / Q000032:analysis*; D013696:Temperature
D012346:RNA, Transfer, Amino Acyl; D008345:Manganese; D008274:Magnesium