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.
Type de document :
Article dans une revue
Biochimie, Elsevier, 2009, 91 (8), pp.1003-9. 〈10.1016/j.biochi.2009.05.004〉
Liste complète des métadonnées

http://www.hal.inserm.fr/inserm-00420164
Contributeur : Maité Peney <>
Soumis le : lundi 28 septembre 2009 - 13:09:19
Dernière modification le : mercredi 14 mars 2018 - 16:41:42

Identifiants

Collections

Citation

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〉

Partager

Métriques

Consultations de la notice

105