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For D. Gandini Attardi and G.P. Tocchini-Valentini,
Trans-acting RNA inhibits tRNA suppressor activity in vivo,
RNA 8:904–912. Due to authors' oversight, the
following statement was inadvertently omitted from the Acknowledgments:
“This work has been supported by Progetto Strategico Genetica
Molecolare Legge 449/97; Programma Biomolecole per la Salute Umana
MURST-CNR Legge 95/95 5%; Progetto Strategico Tecnologie di Base della
Post Genomica (CNR).”
We constructed two aptamers, each of which contains a 7-nt-long
loop complementary to the anticodon loop of a suppressor tRNA.
One of these aptamers can form a stable bimolecular complex
with the suppressor tRNA in vitro and protects the 7 nt in the
suppressor's anticodon loop from RNase S1. An Escherichia
coli strain, carrying an amber mutation in the lac Z gene,
produces β-galactosidase only if the suppressor is present;
the aptamer's coexpression in the cell inhibits the activity
of the suppressor tRNA. Moreover, in E. coli extract,
the aptamer partially inhibits the read-through of the stop
codon on the part of the suppressor tRNA. These results point
to a novel strategy that need not be limited to the suppressor
tRNA. By constructing appropriate inducible aptamers, it may
well be possible to effectively control translation in vivo.
We report the evolution of an RNA aptamer to change
its binding specificity. RNA aptamers that bind the free
amino acid tyrosine were in vitro selected from a degenerate
pool derived from a previously selected dopamine aptamer.
Three independent sequences bind tyrosine in solution,
the winner of the selection binding with a dissociation
constant of 35 μM. Competitive affinity chromatography
with tyrosine-related ligands indicated that the selected
aptamers are highly L-stereo selective and also recognize
L-tryptophan and L-dopa with similar affinity. The binding
site was localized by sequence comparison, analysis of
minimal boundaries, and structural probing upon ligand
binding. Tyrosine-binding sites are characterized by the
presence of both tyrosine (UAU and UAC) and termination
(UAG and UAA) triplets.
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