Barbara Bardoni, PhD
Principal Investigator
CNRS, Nice
France

FRAXA Award:
  $30,000 in 2005  

by Bardoni Bardoni, 8/2004

FMRP is a RNA-binding protein containing at least three domains mediating its binding to RNA (two KH domains and one RGG box) and it appears to be implicated in several steps of mRNA metabolism. These properties suggest that it is likely a component of different complexes, whose identification will result in a more precise dissection of FMRP function. We plan to use sucrose gradient fractionation and FPLC chromatography with the purpose to perform a detailed analysis of FMRP-containing complexes in cultured cell lines and mouse brain, taking into consideration the composition and the dynamics of FMRP-containing complexes, the expression of FMRP-interacting proteins and, as a more long term project, the expression level of mRNAs that are targets of FMRP.

Another important point is to clearly elucidate the anatomy of the FMRP/mRNA complex at the molecular level. During the last four years, many putative RNA targets for FMRP have been identified. However, up to date, it has been reported that FMRP binds only two structures (G-quartet and kissing complex RNA) and a sequence (poly(U) stretch). We propose here a novel approach to identify sequence and/or structures, other than purine-quartet, that are recognized and bound by FMRP.