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.