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

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

  • Biochimie. 2009 Aug;91(8):1003-9. doi: 10.1016/j.biochi.2009.05.004.
Vincent Oliéric 1,  Philippe Wolff,  Akiko Takeuchi,  Guillaume Bec,  Catherine Birck,  Marc Vitorino,  Bruno Kieffer,  Artemy Beniaminov,  Giorgio Cavigiolio,  Elizabeth Theil,  Christine Allmang,  Alain Krol,  Philippe Dumas
Affiliations

Affiliation

  • 1 Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, IBMC, France.
PMID: 19467292 DOI: 10.1016/j.biochi.2009.05.004
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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