Two different combinations of RNA-binding domains determine the RNA-binding specificity of nucleolin

doi:10.1074/jbc.M011120200

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Papers In Press, published online ahead of print January 18, 2001
J. Biol. Chem, 10.1074/jbc.M011120200
Submitted on December 11, 2000
Revised on January 9, 2001
Accepted on January 18, 2001

Two different combinations of RNA-binding domains determine the RNA-binding specificity of nucleolin

Herve Ginisty, Francois Amalric, and Philippe Bouvet

Ecole Normale Superieure de Lyon, CNRS UMR 5665, 69364, Lyon

Corresponding Author: pbouvet{at}ens-lyon.fr

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 (NRE) found all along the pre-ribosomal RNA. The second is a short single stranded RNA sequence (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 RBD?s for the interaction with an RNA target demonstrating that a single protein can use different combinations of RBD to interact specifically with several RNA sequences.

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