Nucleic Acids Research Advance Access originally published online on December 14, 2006
Nucleic Acids Research 2007 35(1):299-306; doi:10.1093/nar/gkl1021
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Nucleic Acids Research, 2007, Vol. 35, No. 1 299-306
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Fragile X related protein 1 isoforms differentially modulate the affinity of fragile X mental retardation protein for G-quartet RNA structure
CNRS UMR 6543, Faculté de Médecine–Université de Nice Sophia-Antipolis 28 Avenue De Valombrose, 06107, Nice, France 1 Unité de Recherche en Génétique Humaine et Moléculaire, Centre de Recherche Hôpital Saint-François d'Assise le CHUQ, Québec, Canada G1L 3L5, Département de Biologie Médicale, Faculté de Médecine, Université Laval, Québec, Canada 2 Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UMR6097 Université de Nice Sophia-Antipolis, 660 Route des Lucioles, 06560 Valbonne Sophia-Antipolis, France
*To whom correspondence should be addressed. Tel: +0033 493377786; Fax: +0033 493377033; Email: bardoni{at}unice.fr
Received September 6, 2006. Revised November 13, 2006. Accepted November 13, 2006.
Fragile X syndrome, the most frequent form of inherited mental retardation, is due to the absence of expression of the Fragile X Mental Retardation Protein (FMRP), an RNA binding protein with high specificity for G-quartet RNA structure. FMRP is involved in several steps of mRNA metabolism: nucleocytoplasmic trafficking, translational control and transport along dendrites in neurons. Fragile X Related Protein 1 (FXR1P), a homologue and interactor of FMRP, has been postulated to have a function similar to FMRP, leading to the hypothesis that it can compensate for the absence of FMRP in Fragile X patients. Here we analyze the ability of three isoforms of FXR1P, expressed in different tissues, to bind G-quartet RNA structure specifically. Only the longest FXR1P isoform was found to be able to bind specifically the G-quartet RNA, albeit with a lower affinity as compared to FMRP, whereas the other two isoforms negatively regulate the affinity of FMRP for G-quartet RNA. This result is important to decipher the molecular basis of fragile X syndrome, through the understanding of FMRP action in the context of its multimolecular complex in different tissues. In addition, we show that the action of FXR1P is synergistic rather than compensatory for FMRP function.
Present address: Laetitia Davidovic, CNRS UMR 6543, Faculté de Médecine–Université de Nice Sophia-Antipolis, 28 Avenue De Valombrose, 06107, Nice, France
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