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Published online 19 April 2004

Nucleic Acids Research, 2004, Vol. 32, No. 7 2129-2137
© 2004 Oxford University Press

The fragile X mental retardation protein has nucleic acid chaperone properties

Caroline Gabus, Rachid Mazroui1, Sandra Tremblay1, Edouard W. Khandjian1 and Jean-Luc Darlix*

LaboRetro, Unité INSERM de Virologie Humaine (412), ENS, 46 allée d’Italie, 69364 Lyon cedex 07, France and 1 Unité de recherche en Génétique Humaine et Moléculaire, Centre de recherche Hôpital St. François d’Assise, CHUQ, 10 rue de l’Espinay, Québec G1L 3L5, PQ Canada

*To whom correspondence should be addressed\. Tel: +33 4 72 72 81 69; Fax: +33 4 72 72 87 77; Email: jldarlix{at}ens-lyon.fr
+AF362952, AF503620, AY429654, AY429655 and TPA BK001786

Received February 9, 2004; Revised and Accepted March 22, 2004

The fragile X syndrome is the most common cause of inherited mental retardation resulting from the absence of the fragile X mental retardation protein (FMRP). FMRP contains two K-homology (KH) domains and one RGG box that are landmarks characteristic of RNA-binding proteins. In agreement with this, FMRP associates with messenger ribonucleoparticles (mRNPs) within actively translating ribosomes, and is thought to regulate translation of target mRNAs, including its own transcript. To investigate whether FMRP might chaperone nucleic acid folding and hybridization, we analysed the annealing and strand exchange activities of DNA oligonucleotides and the enhancement of ribozyme-directed RNA substrate cleavage by FMRP and deleted variants relative to canonical nucleic acid chaperones, such as the cellular YB-1/p50 protein and the retroviral nucleocapsid protein HIV-1 NCp7. FMRP was found to possess all the properties of a potent nucleic acid chaperone, requiring the KH motifs and RGG box for optimal activity. These findings suggest that FMRP may regulate translation by acting on RNA–RNA interactions and thus on the structural status of mRNAs.


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