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Journal articles
SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein.
Vincent Oliéric
1
Philippe Wolff
1
Akiko Takeuchi
1
Guillaume Bec
1
Catherine Birck
2
Marc Vitorino
2
Bruno Kieffer
2
Artemy Beniaminov
1, 3
Giorgio Cavigiolio
4
Elizabeth Theil
4, 5
Christine Allmang
1
Alain Krol
1
Philippe Dumas
1
Catherine Birck 2
Author
Marc Vitorino 2
Author
Bruno Kieffer 2
Author
Artemy Beniaminov 1, 3
Author
Giorgio Cavigiolio 4
Author
Elizabeth Theil 4, 5
Author
Christine Allmang 1
Author
Alain Krol 1
Author
Philippe Dumas 1
Author
1
ARN - Architecture et réactivité de l'ARN (Institut de Biologie Moléculaire et Cellulaire 15 rue René Descartes 67084 STRASBOURG Cedex - France)
- Université Louis Pasteur - Strasbourg I (France)
- CNRS - Centre National de la Recherche Scientifique : UPR9002 (France)
2
IGBMC - Institut de Génétique et de Biologie Moléculaire et Cellulaire (Parc D'Innovation 1 Rue Laurent Fries - BP 10142 67404 Illkirch Cedex - France)
- UNISTRA - Université de Strasbourg : UMR7104 (4 rue Blaise Pascal - CS 90032 - 67081 Strasbourg cedex - France)
- INSERM - Institut National de la Santé et de la Recherche Médicale : U1258 (101, rue de Tolbiac, 75013 Paris - France)
- CNRS - Centre National de la Recherche Scientifique : UMR7104 (France)
3
ISTC - Engelhardt Institute of Molecular Biology (32, ul. Vavilova, 119991 Moscow - Russia)
- RAS - Russian Academy of Sciences [Moscow] (Leninsky Ave, 14, Moscow, Russie, 119991 - Russia)
4
CHORI - Children's Hospital Oakland Research Institute (5700 Martin Luther King Jr. Way, Oakland, CA 94609 - United States)
- CHORI (France)
5
NST - Department of Nutritional Sciences and Toxicology [Berkeley] (University of California Berkeley, CA - United States)
- University of California [Berkeley] (Berkeley, CA - United States)
- University of California (United States)
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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Journal articles
Complete list of metadatas
https://www.hal.inserm.fr/inserm-00420164
Contributor : Maité Peney <>
Submitted on : Monday, September 28, 2009 - 1:09:19 PM
Last modification on : Tuesday, July 14, 2020 - 11:04:04 AM
Contributor : Maité Peney <>
Submitted on : Monday, September 28, 2009 - 1:09:19 PM
Last modification on : Tuesday, July 14, 2020 - 11:04:04 AM
Identifiers
- HAL Id : inserm-00420164, version 1
- DOI : 10.1016/j.biochi.2009.05.004
- PUBMED : 19467292
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CNRS | IGBMC | SITE-ALSACE
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⟩
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