TY - JOUR
T1 - Identification of the metal ion binding site on an RNA motif from hammerhead ribozymes using 15N NMR spectroscopy
AU - Tanaka, Yoshiyuki
AU - Kojima, Chojiro
AU - Morita, Eugene H.
AU - Kasai, Yasuhiro
AU - Yamasaki, Kazuhiko
AU - Ono, Akira
AU - Kainosho, Masatsune
AU - Taira, Kazunari
PY - 2002/5/1
Y1 - 2002/5/1
N2 - An RNA oligomer, r(GGACGAGUCC), which mimics the metal ion-binding motif of hammerhead ribozymes, was shown to fold by itself into a conformation possessing a metal ion binding property which is similar to that of the intact ribozyme (Tanaka, et al. J. Am. Chem. Soc. 2000, 122, 11303-11310). To determine the metal ion-binding site of this motif at an atomic level, we synthesized a series of RNA oligomers which were selectively labeled with a 15N-labeled guanosine at each of the four guanosine residues. The 15N-chemical shift perturbation with Cd(II) ions by one-dimensional (1 D) 15N NMR spectra showed that the chemical shift of the N7 of the G7 residue, N7/G7, in the metal ion-binding motif was specifically perturbed. This is the first experimental evidence to prove that the N7/G7 binds with a Cd(II) ion.
AB - An RNA oligomer, r(GGACGAGUCC), which mimics the metal ion-binding motif of hammerhead ribozymes, was shown to fold by itself into a conformation possessing a metal ion binding property which is similar to that of the intact ribozyme (Tanaka, et al. J. Am. Chem. Soc. 2000, 122, 11303-11310). To determine the metal ion-binding site of this motif at an atomic level, we synthesized a series of RNA oligomers which were selectively labeled with a 15N-labeled guanosine at each of the four guanosine residues. The 15N-chemical shift perturbation with Cd(II) ions by one-dimensional (1 D) 15N NMR spectra showed that the chemical shift of the N7 of the G7 residue, N7/G7, in the metal ion-binding motif was specifically perturbed. This is the first experimental evidence to prove that the N7/G7 binds with a Cd(II) ion.
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U2 - 10.1021/ja011520c
DO - 10.1021/ja011520c
M3 - Article
C2 - 11971706
AN - SCOPUS:0036569818
VL - 124
SP - 4595
EP - 4601
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 17
ER -