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J. Biol. Chem., Vol. 269, Issue 51, 32221-32225, Dec, 1994
S Nakanishi, T Ueda, H Hori, N Yamazaki, N Okada and K Watanabe
Escherichia coli tRNA-guanine transglycosylase is an enzyme which catalyzes
replacement of guanine (G34) of tRNA(Asp), tRNA(Asn), tRNA(His) and
tRNA(Tyr) by free guanine or free preQ1 base by a base exchange reaction in
the biosynthesis of queuosine (Q) (Okada, N., and Nishimura, S. (1979) J.
Biol. Chem. 254, 3061-3066). The gene encoding for this enzyme was
amplified from the E. coli genome by polymerase chain reaction and inserted
into an overexpression vector, pJLA503. The enzyme was overexpressed by
heat induction in E. coli transformed by this recombinant plasmid and
purified to homogeneity by two column chromatographies. The sequence
requirement in tRNA for recognition by this enzyme was investigated using
minihelices corresponding to the anti-codon arm of E. coli tRNA(His). Two
uridine residues (U33, U35) were found to be prerequisite for such
recognition by this enzyme. Position 32 required pyrimidines, because the
enzyme activity toward the minihelices was markedly reduced or entirely
lost when this residue was replaced by purines or was deleted. Adenosine at
position 37 and the G30-C40 base pair were not essential despite their
conservation. Our results suggest that the enzyme recognizes the
U33-G34-U35 sequence in the anti-codon loop and not the tertiary structure
of tRNA itself.
A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNA-guanine transglycosylase
Department of Chemistry and Biotechnology, Faculty of Engineering, University of Tokyo, Japan.
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