SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. - Archive ouverte HAL Access content directly
Journal Articles Biochimie Year : 2009

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

(1) , (1) , (1) , (1) , (2) , (2) , (2) , (1, 3) , (4) , (4, 5) , (1) , (1) , (1)
1
2
3
4
5

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.
Not file

Dates and versions

inserm-00420164 , version 1 (28-09-2009)

Identifiers

Cite

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, 2009, 91 (8), pp.1003-9. ⟨10.1016/j.biochi.2009.05.004⟩. ⟨inserm-00420164⟩
109 View
0 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More