SECIS-binding protein 2, a key player in selenoprotein synthesis,is an intrinsically disordered protein |
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| Authors: | Vincent Olié ric,Philippe Wolff,Akiko Takeuchi,Guillaume Bec,Catherine Birck,Marc Vitorino,Bruno Kieffer,Artemy Beniaminov,Giorgio Cavigiolio,Elizabeth Theil,Christine Allmang,Alain Krol,Philippe Dumas |
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| Affiliation: | 1. Architecture et Réactivité de l''ARN, Université de Strasbourg, CNRS, IBMC, 67084 Strasbourg, France;2. Institut de Génétique et de Biologie Moléculaire et Cellulaire, CEBGS, 1 rue Laurent Fries, BP 10142, 67404 Illkirch Cedex, France;3. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov Street, Moscow 119991, Russia;4. CHORI Children''s Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, USA;5. Department of Nutritional Sciences and Toxicology, University of California, Berkeley, CA 94720, USA |
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| Abstract: | Selenocysteine (Sec) is co-translationally incorporated into selenoproteins at a reprogrammed UGA codon. In mammals, this requires a dedicated machinery comprising a stem-loop structure in the 3′ UTR RNA (the SECIS element) and the specific SECIS Binding Protein 2. In this report, disorder-prediction methods and several biophysical techniques showed that ca. 70% of the SBP2 sequence is disordered, whereas the RNA binding domain appears to be folded and functional. These results are consistent with a recent report on the role of the Hsp90 chaperone for the folding of SBP2 and other functionally unrelated proteins bearing an RNA binding domain homologous to SBP2. |
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| Keywords: | Selenocysteine Recoding SBP2 SECIS Intrinsically disordered protein |
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