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Modèles Insectes d’Immunité Innée
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1996
Hubert N, Walczak R, Sturchler C, Myslinski E, Schuster C, Westhof E, Carbon P, Krol A
RNAs mediating cotranslational insertion of selenocysteine in eukaryotic selenoproteins Article de journal
Dans: Biochimie, vol. 78, no. 7, p. 590-596, 1996, ISBN: 8955902, (0300-9084 Journal Article Review Review, Tutorial).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid-Specific/chemistry/metabolism Rats Schistosoma mansoni Selenocysteine/chemistry/*metabolism Support, Animals Base Sequence Cattle Escherichia coli Human Mice Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Proteins/chemistry/*metabolism RNA/chemistry/*metabolism RNA, Non-U.S. Gov't Xenopus laevis, Transfer, Unité ARN
@article{,
title = {RNAs mediating cotranslational insertion of selenocysteine in eukaryotic selenoproteins},
author = {N Hubert and R Walczak and C Sturchler and E Myslinski and C Schuster and E Westhof and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8955902},
isbn = {8955902},
year = {1996},
date = {1996-01-01},
journal = {Biochimie},
volume = {78},
number = {7},
pages = {590-596},
abstract = {Selenocysteine, a selenium-containing analog of cysteine, is found in the prokaryotic and eukaryotic kingdoms in active sites of enzymes involved in oxidation-reduction reactions. Its biosynthesis and cotranslational insertion into selenoproteins is performed by an outstanding mechanism, implying the participation of several gene products. The tRNA(Sec) is one of these. In eukaryotes, its transcription mode by RNA polymerase III differs from that of classical tRNA genes, both at the level of the promoter elements and transcription factors involved. In addition, enhanced transcription is afforded by a newly characterized zinc finger activator. Not only transcription of the gene, but also the tRNA(Sec) itself is atypical since its 2D and 3D structures exhibit features which set it apart from classical tRNAs. Decoding of eukaryotic selenocysteine UGA codons requires a stem-loop structure in the 3'UTR of mRNAs, the selenocysteine insertion sequence (SECIS) element. Structure probing and sequence comparisons led us to propose a 2D structure model for the SECIS element, containing a novel RNA motif composed of four consecutive non-Watson-Crick base-pairs. A 3D model, rationalizing the accessibility data, was elaborated by computer modeling. It yields indicative or suggestive evidence for the role that could play some conserved residues and/or structural features in SECIS function. These might act as signals for interaction with SBP, the SECIS binding protein that we have characterized.},
note = {0300-9084
Journal Article
Review
Review, Tutorial},
keywords = {Amino Acid-Specific/chemistry/metabolism Rats Schistosoma mansoni Selenocysteine/chemistry/*metabolism Support, Animals Base Sequence Cattle Escherichia coli Human Mice Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Proteins/chemistry/*metabolism RNA/chemistry/*metabolism RNA, Non-U.S. Gov't Xenopus laevis, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Selenocysteine, a selenium-containing analog of cysteine, is found in the prokaryotic and eukaryotic kingdoms in active sites of enzymes involved in oxidation-reduction reactions. Its biosynthesis and cotranslational insertion into selenoproteins is performed by an outstanding mechanism, implying the participation of several gene products. The tRNA(Sec) is one of these. In eukaryotes, its transcription mode by RNA polymerase III differs from that of classical tRNA genes, both at the level of the promoter elements and transcription factors involved. In addition, enhanced transcription is afforded by a newly characterized zinc finger activator. Not only transcription of the gene, but also the tRNA(Sec) itself is atypical since its 2D and 3D structures exhibit features which set it apart from classical tRNAs. Decoding of eukaryotic selenocysteine UGA codons requires a stem-loop structure in the 3'UTR of mRNAs, the selenocysteine insertion sequence (SECIS) element. Structure probing and sequence comparisons led us to propose a 2D structure model for the SECIS element, containing a novel RNA motif composed of four consecutive non-Watson-Crick base-pairs. A 3D model, rationalizing the accessibility data, was elaborated by computer modeling. It yields indicative or suggestive evidence for the role that could play some conserved residues and/or structural features in SECIS function. These might act as signals for interaction with SBP, the SECIS binding protein that we have characterized.