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J. Biol. Chem., Vol. 276, Issue 25, 22844-22849, June 22, 2001
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From the Institute of Biological Sciences, University of Tsukuba,
Tsukuba-shi, Ibaraki 305-8572, Japan and the § Department of
Industrial Chemistry, Chiba Institute of Technology, 2-17-1 Tsudanuma,
Narashino-shi, Chiba 275-0016, Japan
Escherichia coli cells contain abundant
amounts of metabolically stable 4.5 S RNA. Consisting of 114 nucleotides, 4.5 S RNA is structurally homologous to mammalian 7 S RNA,
and it plays an essential role in targeting proteins containing signal
peptide to the secretory apparatus by forming an signal
recognition-like particle with Ffh protein. It also binds
independently to protein elongation factor G (EF-G) and functions in
the translation process. This RNA contains a phylogenetically conserved
RNA domain, the predicted secondary structure of which consists of a
hairpin motif with two bulges. We examined the binding activity of
mutants with systematic deletions to define the minimal functional
interaction domain of 4.5 S RNA that interacts with EF-G. This domain
consisted of 35-nucleotides extending from 36 to 70 nucleotides of
mature 4.5 S RNA and contained two conserved bulges in which mutations of A47, A60, G61, C62, A63, and A67 diminished binding to EF-G, whereas
those at A39, C40, C41, A42, G48, and G49 did not affect binding. These
data suggested that the 10 nucleotides in 4.5 S RNA, which are
conserved between 4.5 S RNA and 23 S rRNA, have a key role for EF-G
binding. Based on the NMR-derived structure of mutant A47U, we further
verified that substituting U at A47 causes striking structural changes
and the loss of the symmetrical bulge. These results indicate the
mechanism by which EF-G interacts with 4.5 S RNA and the importance of
the bulge structure for EF-G binding.
Minimal Functional Structure of Escherichia
coli 4.5 S RNA Required for Binding to Elongation Factor G*
,
*
This work was supported by a grant-in-aid for scientific
research from the Ministry of Education, Science and Sports, and Culture of Japan, by Mitsubishi Chemical Corporation Fund, and in part
by the "Research for the Future" program (JSPS-RFTF97L00503) from
the Japan Society for the Promotion of Science.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel. and Fax:
+81-298-53-6006; E-mail: nakamura.kouji@nifty.ne.jp.
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