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SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein.

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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https://www.hal.inserm.fr/inserm-00420164
Contributor : Maité Peney <>
Submitted on : Monday, September 28, 2009 - 1:09:19 PM
Last modification on : Tuesday, July 14, 2020 - 11:04:04 AM

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Vincent Oliéric, Philippe Wolff, Akiko Takeuchi, Guillaume Bec, Catherine Birck, et al.. SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein.. Biochimie, Elsevier, 2009, 91 (8), pp.1003-9. ⟨10.1016/j.biochi.2009.05.004⟩. ⟨inserm-00420164⟩

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