Nucleic Acids Research, Vol 27, Issue 24 4743-4750, Copyright © 1999 by Oxford University Press
YM Hou, H Motegi, RS Lipman, CS Hamann and K Shiba
The core region of Escherichia coli tRNA(Cys)is important for
aminoacylation of the tRNA. This core contains an unusual G15:G48 base
pair, and three adenosine nucleotides A13, A22 and A46 that are likely to
form a 46:[13:22] adenosine base triple. We recently observed that the
15:48 base pair and the proposed 46:[13:22] triple are structurally and
functionally coupled to contribute to aminoacylation. Inspection of a
database of tRNA sequences shows that these elements are only found in one
other tRNA, the Haemophilus influenzae tRNA(Cys). Because of the complexity
of the core, conservation of sequence does not mean conservation of
function. We here tested whether the conserved elements in H. influenzae
tRNA(Cys)were also important for aminoacylation of H. influenzae tRNA(Cys).
We cloned and purified a recombinant H. influenzae cysteine-tRNA
synthe-tase and showed that it depends on 15:48 and 13, 22 and 46 in a
relationship analogous to that of E. coli cysteine-tRNA synthetase. The
functional conservation of the tRNA core is correlated with sequence
conservation between E.coli and H.influenzae cysteine-tRNA synthetases. As
the genome of H. influenzae is one of the smallest and may approximate a
small autonomous entity in the development of life, the dependence of this
genome on G15:G48 and its coupling with the proposed A46:[A13:A22] triple
for aminoacylation with cysteine suggests an early role of these motifs in
the evolution of decoding genetic information.
ARTICLES
Conservation of a tRNA core for aminoacylation
Thomas Jefferson University, Department of Biochemistry, 233 South 10th Street, Room 222, Philadelphia, PA 19107, USA.
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