TY - JOUR
T1 - Sequence/structure selective thermal and photochemical cleavage of yeast-tRNA(Phe) by UO(2)2+
AU - Nielsen, Peter E.
AU - Møllegaard, N E
N1 - Keywords: Hot Temperature; Nucleic Acid Conformation; Photochemistry; RNA, Fungal; RNA, Transfer, Phe; Saccharomyces cerevisiae; Uranium Compounds
PY - 1997
Y1 - 1997
N2 - The uranyl(VI) ion, UO(2)2+, cleaves yeast tRNA(Phe) both thermally and photochemically. Photochemical cleavage takes place at all positions but exhibits maxima at G10, G18, G30, A38, C49 and A62. Furthermore, in the presence of stoichiometric concentrations of citrate, the cleavage is generally suppressed except that strong cleavage at positions G10 and C48-U50 persists, indicating the presence of a high-affinity metal-ion binding site. It is proposed that these photocleavage sites reflect the tertiary structure of the yeast tRNA(Phe) molecule in terms of D-loop/T-loop interaction and anticodon loop conformation and that uranyl-mediated photocleavage of RNA may be used as a probe of RNA tertiary structure, and in particular for identifying binding sites for divalent metal ions. Thus a high-affinity metal-ion binding site is inferred in the "central pocket" formed by the D-loop, and the acceptor stem.
AB - The uranyl(VI) ion, UO(2)2+, cleaves yeast tRNA(Phe) both thermally and photochemically. Photochemical cleavage takes place at all positions but exhibits maxima at G10, G18, G30, A38, C49 and A62. Furthermore, in the presence of stoichiometric concentrations of citrate, the cleavage is generally suppressed except that strong cleavage at positions G10 and C48-U50 persists, indicating the presence of a high-affinity metal-ion binding site. It is proposed that these photocleavage sites reflect the tertiary structure of the yeast tRNA(Phe) molecule in terms of D-loop/T-loop interaction and anticodon loop conformation and that uranyl-mediated photocleavage of RNA may be used as a probe of RNA tertiary structure, and in particular for identifying binding sites for divalent metal ions. Thus a high-affinity metal-ion binding site is inferred in the "central pocket" formed by the D-loop, and the acceptor stem.
U2 - 10.1002/(SICI)1099-1352(199605)9:3<228::AID-JMR243>3.0.CO;2-R
DO - 10.1002/(SICI)1099-1352(199605)9:3<228::AID-JMR243>3.0.CO;2-R
M3 - Journal article
C2 - 8938595
SN - 0952-3499
VL - 9
SP - 228
EP - 232
JO - Journal of Molecular Recognition
JF - Journal of Molecular Recognition
IS - 3
ER -