Nucleic Acids Research, Vol 25, Issue 11 2083-2090, Copyright © 1997 by Oxford University Press
A Ramos and G Varani
The fidelity of translation of the genetic code depends on accurate tRNA
aminoacylation by cognate aminoacyl-tRNA synthetases. Thus, each tRNA has
specificity not only for codon recognition, but also for amino acid
identity; this aminoacylation specificity is referred to as tRNA identity.
The primary determinant of the acceptor identity of Escherichia coli
tRNAAlais a wobble G3.U70 pair within the acceptor stem. Despite extensive
biochemical and genetic data, the mechanism by which the G3.U70 pair marks
the acceptor end of tRNAAla for aminoacylation with alanine has not been
clarified at the molecular level. The solution structure of a microhelix
derived from the tRNAAla acceptor end has been determined at high precision
using a very extensive set of experimental constraints (approximately 32
per nt) obtained by heteronuclear multidimensional NMR methods. The tRNAAla
acceptor end is overall similar to A-form RNA, but important differences
are observed. The G3.U70 wobble pair distorts the conformation of the
phosphodiester backbone and presents the functional groups of U70 in an
unusual spatial location. The discriminator base A73 has extensive stacking
overlap with G1 within the G1.C72 base pair at the end of the double
helical stem and the -CCA end is significantly less ordered than the rest
of the molecule.
ARTICLES
Structure of the acceptor stem of Escherichia coli tRNA Ala: role of the G3.U70 base pair in synthetase recognition
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
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