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Modèles Insectes d’Immunité Innée
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1994
Baron C, Sturchler C, Wu X Q, Gross H J, Krol A, Bock A
Eukaryotic selenocysteine inserting tRNA species support selenoprotein synthesis in Escherichia coli Article de journal
Dans: Nucleic Acids Res, vol. 22, no. 12, p. 2228-2233, 1994, ISBN: 8036149, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid-Specific/chemistry/*genetics Selenocysteine/chemistry Serine-tRNA Ligase/metabolism Support, Animals Bacterial Proteins/metabolism Base Sequence Cloning, Molecular Escherichia coli/*genetics Genetic Complementation Test Human Nucleic Acid Conformation Peptide Elongation Factors/metabolism Proteins/*biosynthesis/genetics RNA, Non-U.S. Gov't Xenopus laevis, Transfer, Unité ARN
@article{,
title = {Eukaryotic selenocysteine inserting tRNA species support selenoprotein synthesis in Escherichia coli},
author = {C Baron and C Sturchler and X Q Wu and H J Gross and A Krol and A Bock},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8036149},
isbn = {8036149},
year = {1994},
date = {1994-01-01},
journal = {Nucleic Acids Res},
volume = {22},
number = {12},
pages = {2228-2233},
abstract = {Although the tRNA species directing selenocysteine insertion in prokaryotes differ greatly in their primary structure from that of their eukaryotic homologues they share very similar three-dimensional structures. To analyse whether this conservation of the overall shape of the molecules reflects a conservation of their functional interactions it was tested whether the selenocysteine inserting tRNA species from Homo sapiens supports selenoprotein synthesis in E. coli. It was found that the expression of the human tRNA(Sec) gene in E.coli can complement a lesion in the tRNA(Sec) gene of this organism. Transcripts of the Homo sapiens and Xenopus laevis tRNA(Sec) genes synthesised in vitro were amino-acylated by the E.coli seryl-tRNA ligase although at a very low rate and the resulting seryl-tRNA(Sec) was bound to and converted into selenocysteyl-tRNA(Sec) by the selenocysteine synthase of this organism. Selenocysteyl-tRNA(Sec) from both eukaryotes was able to form a complex with translation factor SELB from E.coli. Although the mechanism of selenocysteine incorporation into seleno-proteins appears to be rather different in E.coli and in vertebrates, we observe here a surprising conservation of functions over an enormous evolutionary distance.},
note = {0305-1048
Journal Article},
keywords = {Amino Acid-Specific/chemistry/*genetics Selenocysteine/chemistry Serine-tRNA Ligase/metabolism Support, Animals Bacterial Proteins/metabolism Base Sequence Cloning, Molecular Escherichia coli/*genetics Genetic Complementation Test Human Nucleic Acid Conformation Peptide Elongation Factors/metabolism Proteins/*biosynthesis/genetics RNA, Non-U.S. Gov't Xenopus laevis, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Although the tRNA species directing selenocysteine insertion in prokaryotes differ greatly in their primary structure from that of their eukaryotic homologues they share very similar three-dimensional structures. To analyse whether this conservation of the overall shape of the molecules reflects a conservation of their functional interactions it was tested whether the selenocysteine inserting tRNA species from Homo sapiens supports selenoprotein synthesis in E. coli. It was found that the expression of the human tRNA(Sec) gene in E.coli can complement a lesion in the tRNA(Sec) gene of this organism. Transcripts of the Homo sapiens and Xenopus laevis tRNA(Sec) genes synthesised in vitro were amino-acylated by the E.coli seryl-tRNA ligase although at a very low rate and the resulting seryl-tRNA(Sec) was bound to and converted into selenocysteyl-tRNA(Sec) by the selenocysteine synthase of this organism. Selenocysteyl-tRNA(Sec) from both eukaryotes was able to form a complex with translation factor SELB from E.coli. Although the mechanism of selenocysteine incorporation into seleno-proteins appears to be rather different in E.coli and in vertebrates, we observe here a surprising conservation of functions over an enormous evolutionary distance.