CHED 846 |
| The most common form of inherited mental retardation is the Fragile X syndrome, which is an X-linked recessive trait caused by the expansion of a trinucleotide CGG repeat in the fragile X mental retardation 1 (FMR1) gene. The fragile X mental retardation protein (FMRP) has been proposed to bind to messenger RNAs that form G quadruplex structures. One such RNA is semaphorin 3F (S3F) mRNA, which encodes for a protein involved in the guidance of growth cones during neuronal extension. S3F RNA has been proposed to interact with FMRP via the recognition of its G quadruplex structure. In this study we demonstrate that S3F RNA folds into an intramolecular parallel G quadruplex structure to which the FMRP RGG Box domain binds with high affinity and specificity, by using fluorescence, UV, circular dichroism and NMR spectroscopy. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |