Recently, two RNA structural motifs, the interdigitated T-loop (ITL) and metastasisassociated lung adenocarcinoma transcript1 triple helix (MALAT1 TH), were discovered with important biological roles. The ITL motif is responsible for binding the tRNA elbow to control the structural orientation of tRNA in various biochemical and regulatory processes. The triple helix protects the MALAT1 transcript, which is upregulated in many cancerous tissues, from 3’ exonuclease degradation pathways. We aim to investigate the molecular details of dynamic conformational properties for these two motifs. Results from our biochemical and biophysical experiments demonstrate that the ITL, though a complex tertiary structure, is highly stable even at low salt concentrations. Moreover, using UV melt experiments on the ITL motif and DSF experiments on MALAT1 TH we characterize the stability of tertiary and secondary structures in both. These results inform the design of high throughput FRET reporter assays appropriate for chemical screening and drug discovery.
|School:||University of the Sciences in Philadelphia|
|School Location:||United States -- Pennsylvania|
|Source:||MAI 56/03M(E), Masters Abstracts International|
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