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J. Biol. Chem., Vol. 276, Issue 17, 14338-14343, April 27, 2001
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From the Laboratoire de Pharmacologie et de Biologie Structurale,
CNRS UMR 5089, 205 route de Narbonne, 31077 Toulouse Cedex,
France and the Nucleolin is an abundant nucleolar protein
involved in several steps of ribosome biogenesis. The protein is highly
conserved through evolution and possesses four RNA-binding domains
(RBD), which are likely to determine its RNA binding specificity.
Previous studies have shown that nucleolin interacts with two different RNA targets. The first is a small stem-loop structure, the nucleolin recognition element (NRE), found all along the pre-ribosomal
RNA. The second is a short single-stranded RNA sequence, the
evolutionary conserved motif (ECM), located five nucleotides
downstream of the first processing site in the pre-ribosomal RNA 5'
external transcribed spacer. Biochemical, genetic, and structural
studies have shown that the first two RBD of nucleolin are necessary
and sufficient for the specific interaction of nucleolin with the NRE
motif. In this work, we have studied the interaction of nucleolin with
the ECM sequence. Deletion and mutational analyses showed that all four
RBDs of hamster nucleolin were required for the interaction with the
ECM sequence. This RNA binding specificity is conserved between hamster
and Xenopus laevis, whereas the Xenopus protein
does not interact with the NRE. Nucleolin is the first example of a
protein that requires four RBDs for its interaction with an RNA target,
demonstrating that a single protein can use different combinations of
RBD to interact specifically with several RNA sequences.
Two Different Combinations of RNA-binding Domains Determine
the RNA Binding Specificity of Nucleolin*
Ecole Normale Supérieure de Lyon,
CNRS UMR 5665, 46 Allée d'Italie, 69364 Lyon Cedex 07, France
*
This work is supported by grants from the Association pour
la Recherche contre le Cancer (ARC), CNRS, and Fondation pour la Recherche Médicale (FRM).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.: 33-4-72-728016;
Fax: 33-4-72-728080; E-mail: pbouvet@ens-lyon.fr.
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