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

被引:8
作者
Olieric, Vincent [1 ]
Wolff, Philippe [1 ]
Takeuchi, Akiko [1 ]
Bec, Guillaume [1 ]
Birck, Catherine [2 ]
Vitorino, Marc [2 ]
Kieffer, Bruno [2 ]
Beniaminov, Artemy [1 ,3 ]
Cavigiolio, Giorgio [4 ]
Theil, Elizabeth [4 ,5 ]
Allmang, Christine [1 ]
Krol, Alain [1 ]
Dumas, Philippe [1 ]
机构
[1] Univ Strasbourg, CNRS, IBMC, Architecture & React ARN, F-67084 Strasbourg, France
[2] CEBGS, Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch Graffenstaden, France
[3] Russian Acad Sci, VA Engelhardt Mol Biol Inst, Moscow 119991, Russia
[4] Childrens Hosp, Oakland Res Inst, Oakland, CA 94609 USA
[5] Univ Calif Berkeley, Dept Nutr Sci & Toxicol, Berkeley, CA 94720 USA
关键词
Selenocysteine; Recoding; SBP2; SECIS; Intrinsically disordered protein; SELENOCYSTEINE INCORPORATION MACHINERY; INSERTION-SEQUENCE BINDING-PROTEIN-2; RNA-BINDING; UNSTRUCTURED PROTEINS; DECODING APPARATUS; ELONGATION-FACTOR; MESSENGER-RNAS; RIBOSOME; DOMAIN; TRANSLATION;
D O I
10.1016/j.biochi.2009.05.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2009 Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:1003 / 1009
页数:7
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