Jenner L, Romby P, Rees B, Schulze-Briese C, Springer M, Ehresmann C, Ehresmann B, Moras D, Yusupova G, Yusupov M
Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding Article de journal
Dans: Science, vol. 308, no. 5718, p. 120-123, 2005, ISBN: 15802605, (1095-9203 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 16S/chemistry/metabolism RNA, Bacterial/*chemistry/metabolism RNA, Messenger/*chemistry/metabolism RNA, Met/chemistry/metabolism *Regulatory Sequences, Molecular Nucleic Acid Conformation *Protein Biosynthesis RNA, Non-U.S. Gov't Ribosomal Proteins/metabolism Ribosomes/*metabolism Thermus thermophilus/genetics/*metabolism Threonine-tRNA Ligase/genetics/metabolism, Ribonucleic Acid Repressor Proteins/*metabolism Research Support, Ribosomal, ROMBY, ROMBY Bacterial Proteins/metabolism Base Pairing Binding Sites Crystallization Crystallography, Transfer, Unité ARN, X-Ray Fourier Analysis Models
@article{,
title = {Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding},
author = {L Jenner and P Romby and B Rees and C Schulze-Briese and M Springer and C Ehresmann and B Ehresmann and D Moras and G Yusupova and M Yusupov},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15802605},
isbn = {15802605},
year = {2005},
date = {2005-01-01},
journal = {Science},
volume = {308},
number = {5718},
pages = {120-123},
abstract = {The ribosome of Thermus thermophilus was cocrystallized with initiator transfer RNA (tRNA) and a structured messenger RNA (mRNA) carrying a translational operator. The path of the mRNA was defined at 5.5 angstroms resolution by comparing it with either the crystal structure of the same ribosomal complex lacking mRNA or with an unstructured mRNA. A precise ribosomal environment positions the operator stem-loop structure perpendicular to the surface of the ribosome on the platform of the 30S subunit. The binding of the operator and of the initiator tRNA occurs on the ribosome with an unoccupied tRNA exit site, which is expected for an initiation complex. The positioning of the regulatory domain of the operator relative to the ribosome elucidates the molecular mechanism by which the bound repressor switches off translation. Our data suggest a general way in which mRNA control elements must be placed on the ribosome to perform their regulatory task.},
note = {1095-9203
Journal Article},
keywords = {16S/chemistry/metabolism RNA, Bacterial/*chemistry/metabolism RNA, Messenger/*chemistry/metabolism RNA, Met/chemistry/metabolism *Regulatory Sequences, Molecular Nucleic Acid Conformation *Protein Biosynthesis RNA, Non-U.S. Gov't Ribosomal Proteins/metabolism Ribosomes/*metabolism Thermus thermophilus/genetics/*metabolism Threonine-tRNA Ligase/genetics/metabolism, Ribonucleic Acid Repressor Proteins/*metabolism Research Support, Ribosomal, ROMBY, ROMBY Bacterial Proteins/metabolism Base Pairing Binding Sites Crystallization Crystallography, Transfer, Unité ARN, X-Ray Fourier Analysis Models},
pubstate = {published},
tppubtype = {article}
}
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}
}