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RNA-protein interaction in the selenoprotein synthesis machinery

Abstract : The 21st amino acid selenocysteine is encoded by a UGA codon that usually signifies translational termination. Selenoprotein synthesis therefore requires specialized factors. Among these is SBP2 that binds the SECIS, a stem-loop structure in the 3'UTR of selenoprotein mRNAs. In structural analyses of SBP2, we isolated and functionally characterized Drosophila melanogaster SBP2. By comparing it with human SBP2, we identified an additional RNA binding domain that is essential for SECIS and 60S ribosomal subunit binding, and also enables SECIS structure selectivity. In addition, computational and biophysical analyses established that SBP2 is globally unfolded, supporting our hypothesis that SBP2 is an Intrinsically Disordered Protein and becomes folded in the presence of partners yet to be identified. Finally, we searched for potential partners of SBP2 and our results showed that the molecular assembly of selenoprotein mRNPs has many similarities with that of sn/snoRNPs.
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Contributor : Isabelle Martin <>
Submitted on : Tuesday, February 9, 2010 - 2:35:20 PM
Last modification on : Thursday, April 23, 2020 - 2:26:32 PM
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  • HAL Id : tel-00455002, version 1



Akiko Takeuchi. RNA-protein interaction in the selenoprotein synthesis machinery. Life Sciences [q-bio]. Université de Strasbourg, 2009. English. ⟨tel-00455002⟩



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