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

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

https://www.ncbi.nlm.nih.gov/pubmed/19467292

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