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- W2005259072 abstract "Pseudouridine at position 39 (Ψ 39 ) of tRNA's anticodon stem and loop domain (ASL) is highly conserved. To determine the physicochemical contributions of Ψ 39 to the ASL and to relate these properties to tRNA function in translation, we synthesized the unmodified yeast tRNA Phe ASL and ASLs with various derivatives of U 39 and Ψ 39 . Ψ 39 increased the thermal stability of the ASL (Δ Tm = 1.3 ± 0.5°C), but did not significantly affect ribosomal binding ( Kd = 229 ± 29 nM) compared to that of the unmodified ASL ( Kd = 197 ± 58 nM). The ASL-Ψ 39 P-site fingerprint on the 30S ribosomal subunit was similar to that of the unmodified ASL. The stability, ribosome binding and fingerprint of the ASL with m 1 Ψ 39 were comparable to that of the ASL with Ψ 39 . Thus, the contribution of Ψ 39 to ASL stability is not related to N1-H hydrogen bonding, but probably is due to the nucleoside's ability to improve base stacking compared to U. In contrast, substitutions of m 3 Ψ 39 , the isosteric m 3 U 39 and m 1 m 3 Ω 39 destabilized the ASL by disrupting the A 31 -U 39 base pair in the stem, as confirmed by NMR. N3-methylations of both U and Ψ dramatically decreased ribosomal binding ( Kd = 1060 ±189 to 1283 ± 258 nM). Thus, canonical base pairing of Ψ 39 to A 31 through N3-H is important to structure, stability and ribosome binding, whereas the increased stability and the N1-proton afforded by modification of U 39 to Ψ 39 may have biological roles other than tRNA's binding to the ribosomal P-site." @default.
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- W2005259072 date "1999-09-01" @default.
- W2005259072 modified "2023-10-10" @default.
- W2005259072 title "Structural and functional roles of the N1- and N3-protons of at tRNA's position 39" @default.
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- W2005259072 doi "https://doi.org/10.1093/nar/27.17.3543" @default.
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