Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1952841 | Biochimie | 2009 | 7 Pages |
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.
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Authors
Vincent Oliéric, Philippe Wolff, Akiko Takeuchi, Guillaume Bec, Catherine Birck, Marc Vitorino, Bruno Kieffer, Artemy Beniaminov, Giorgio Cavigiolio, Elizabeth Theil, Christine Allmang, Alain Krol, Philippe Dumas,