Publications
1994
Philippe C, Benard L, Eyermann F, Cachia C, Kirillov S V, Portier C, Ehresmann B, Ehresmann C
Structural elements of rps0 mRNA involved in the modulation of translational initiation and regulation of E. coli ribosomal protein S15 Article de journal
Dans: Nucleic Acids Res, vol. 22, no. 13, p. 2538-2546, 1994, ISBN: 8041615, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Base Sequence Cloning, Genetic, Messenger/*chemistry/metabolism RNA, Molecular Escherichia coli/*genetics Kinetics Lac Operon Molecular Sequence Data Mutation Nucleic Acid Conformation Operon Protein Binding RNA, Non-U.S. Gov't *Translation, Ribosomal/metabolism Ribosomal Proteins/*genetics Support, Unité ARN
@article{,
title = {Structural elements of rps0 mRNA involved in the modulation of translational initiation and regulation of E. coli ribosomal protein S15},
author = {C Philippe and L Benard and F Eyermann and C Cachia and S V Kirillov and C Portier and B Ehresmann and C Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8041615},
isbn = {8041615},
year = {1994},
date = {1994-01-01},
journal = {Nucleic Acids Res},
volume = {22},
number = {13},
pages = {2538-2546},
abstract = {Previous experiments showed that S15 inhibits its own translation by binding to its mRNA in a region overlapping the ribosome loading site. This binding was postulated to stabilize a pseudoknot structure that exists in equilibrium with two stem-loops and to trap the ribosome on its mRNA loading site in a transitory state. In this study, we investigated the effect of mutations in the translational operator on: the binding of protein S15, the formation of the 30S/mRNA/tRNA(fMet) ternary initiation complex, the ability of S15 to inhibit the formation of this ternary complex. The results were compared to in vivo expression and repression rates. The results show that (1) the pseudoknot is required for S15 recognition and translational control; (2) mRNA and 16S rRNA efficiently compete for S15 binding and 16S rRNA suppresses the ability of S15 to inhibit the formation of the active ternary complex; (3) the ribosome binds more efficiently to the pseudoknot than to the stem-loop; (4) sequences located between nucleotides 12 to 47 of the S15 coding phase enhances the efficiency of ribosome binding in vitro; this is correlated with enhanced in vivo expression and regulation rates.},
note = {0305-1048
Journal Article},
keywords = {Base Sequence Cloning, Genetic, Messenger/*chemistry/metabolism RNA, Molecular Escherichia coli/*genetics Kinetics Lac Operon Molecular Sequence Data Mutation Nucleic Acid Conformation Operon Protein Binding RNA, Non-U.S. Gov't *Translation, Ribosomal/metabolism Ribosomal Proteins/*genetics Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Previous experiments showed that S15 inhibits its own translation by binding to its mRNA in a region overlapping the ribosome loading site. This binding was postulated to stabilize a pseudoknot structure that exists in equilibrium with two stem-loops and to trap the ribosome on its mRNA loading site in a transitory state. In this study, we investigated the effect of mutations in the translational operator on: the binding of protein S15, the formation of the 30S/mRNA/tRNA(fMet) ternary initiation complex, the ability of S15 to inhibit the formation of this ternary complex. The results were compared to in vivo expression and repression rates. The results show that (1) the pseudoknot is required for S15 recognition and translational control; (2) mRNA and 16S rRNA efficiently compete for S15 binding and 16S rRNA suppresses the ability of S15 to inhibit the formation of the active ternary complex; (3) the ribosome binds more efficiently to the pseudoknot than to the stem-loop; (4) sequences located between nucleotides 12 to 47 of the S15 coding phase enhances the efficiency of ribosome binding in vitro; this is correlated with enhanced in vivo expression and regulation rates.