SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein.
Fiche publication
Date publication
août 2009
Auteurs
Membres identifiés du Cancéropôle Est :
Dr BIRCK Catherine, Dr KIEFFER Bruno
Tous les auteurs :
Olieric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P
Lien Pubmed
Résumé
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.
Référence
Biochimie. 2009 Aug;91(8):1003-9