A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1
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2014-05
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Journal Article
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Abstract
The double-stranded RNA-binding domain (dsRBD) is an abundant, conserved RNA-binding motif. Besides RNA binding, dsRBDs can serve as protein-interaction domains. In the human RNA-editing enzyme adenosine deaminase acting on RNA (ADAR1), one of its three dsRBDs mediates nuclear import by interacting with the import receptor transportin 1 (Trn1). RNA binding interferes with Trn1 binding, thereby preventing nuclear import. Using NMR spectroscopy and cell biological analysis, we show that the regions flanking this dsRBD form a bimodular Trn1-dependent nuclear localization signal. The dsRBD itself is not involved in Trn1 interaction but properly positions the Trn1 interacting regions. Using molecular modeling, we provide a structural explanation on how dsRNA binding prevents the dsRBD from accessing the interacting cavity of Trn1, thereby preventing nuclear import of RNA-bound ADAR1.
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published
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111 (18)
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National Academy of Sciences
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Subject
NMR; RNA-binding protein; Nucleocytoplasmic shuttling; RNA deamination
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03591 - Allain, Frédéric / Allain, Frédéric