SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein.
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.
Oliéric
Vincent
V
Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, IBMC, France.
Wolff
Philippe
P
Takeuchi
Akiko
A
Bec
Guillaume
G
Birck
Catherine
C
Vitorino
Marc
M
Kieffer
Bruno
B
Beniaminov
Artemy
A
Cavigiolio
Giorgio
G
Theil
Elizabeth
E
Allmang
Christine
C
Krol
Alain
A
Dumas
Philippe
P
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D051381:Rats; D051140:Selenoproteins / Q000096:biosynthesis*; D017422:Sequence Analysis, DNA
D016601:RNA-Binding Proteins; C498488:Secisbp2 protein, rat; D051140:Selenoproteins