FMRP is Associated to the Ribosomes Via RNA
1996
textabstractThe FMR1 transcript is alternatively spliced and generates different
splice variants coding for FMR1 proteins (FMRP) with a predicted molecular
mass of 70-80 kDa. FMRP is widely expressed and localized in the
cytoplasm. To study a possible interaction with other cellular components,
FMRP was isolated and characterized under non-denaturing conditions. Under
physiological salt conditions FMRP appears to have a molecular mass of >
600 kDa, indicating a binding to other cellular components. This
interaction is disrupted in the presence of high salt concentrations. The
dissociation conditions to free FMRP from the complex are similar to the
dissociation of FMRP from RNA as shown before. The binding of FMRP from
the complex is also disrupted by RNAse treatment. That the association of
FMRP to a high molecular weight complex possibly occurs via RNA, is
further supported by the observation that the binding of FMRP, containing
an lle304Asn substitution, to the high molecular weight complex is
reduced. An equal reduced binding of mutated FMRP to RNA in vitro was
observed before under the same conditions. The reduced binding of FMRP
with the lle304Asn substitution further indicates that the interaction to
the complex indeed occurs via FMRP and not via other RNA binding proteins.
In a reconstitution experiment where the low molecular mass FMRP (70-80
kDa) is mixed with a reticulocyte lysate (enriched in ribosomes) it was
shown that FMRP can associate to ribosomes and that this binding most
likely occurs via RNA.
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