Nucleic Acids Research, Vol 27, Issue 17 3543-3549, Copyright © 1999 by Oxford University Press
CS Yarian, MM Basti, RJ Cain, G Ansari, RH Guenther, E Sochacka, G Czerwinska, A Malkiewicz and PF Agris
Pseudouridine at position 39 (Psi(39)) of tRNA's anticodon stem and loop
domain (ASL) is highly conserved. To determine the physicochemical
contributions of Psi(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 Psi(39). Psi(39)increased the
thermal stability of the ASL (Delta T (m)= 1.3 +/- 0.5 degrees C), but did
not significantly affect ribosomal binding ( K (d)= 229 +/- 29 nM) compared
to that of the unmodified ASL (K (d)= 197 +/- 58 nM). The ASL-Psi(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)Psi(39)were comparable to that of the ASL with Psi(39). Thus, the
contribution of Psi(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)Psi(39), the
isosteric m(3)U(39)and m(1)m(3)Psi(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 Psi dramatically decreased ribosomal binding ( K (d)= 1060
+/- 189 to 1283 +/- 258 nM). Thus, canonical base pairing of Psi(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 Psi(39)may have biological roles other than tRNA's
binding to the ribosomal P-site.
ARTICLES
Structural and functional roles of the N1- and N3-protons of psi at tRNA's position 39
Department of Biochemistry, North Carolina State University, Raleigh, NC 27695, USA,
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