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 Journal Article
In: Science, vol. 308, no. 5718, pp. 120-123, 2005, ISBN: 15802605, (1095-9203 Journal Article).
Abstract | Links | BibTeX | Tags: 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}
}
Westhof E, Massire C
Structural biology. Evolution of RNA architecture Journal Article
In: Science, vol. 306, no. 5693, pp. 62-63, 2004, ISBN: 15459373, (1095-9203 Comment Journal Article).
Links | BibTeX | Tags: Adenine/chemistry Base Pairing Computational Biology Crystallography, Bacterial/*chemistry/metabolism RNA, Molecular Nucleic Acid Conformation RNA Precursors/metabolism RNA, Transfer/metabolism Ribonuclease P/*chemistry/metabolism Thermus thermophilus/*chemistry/enzymology, Unité ARN, WESTHOF, X-Ray Evolution
@article{,
title = {Structural biology. Evolution of RNA architecture},
author = {E Westhof and C Massire},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15459373},
isbn = {15459373},
year = {2004},
date = {2004-01-01},
journal = {Science},
volume = {306},
number = {5693},
pages = {62-63},
note = {1095-9203
Comment
Journal Article},
keywords = {Adenine/chemistry Base Pairing Computational Biology Crystallography, Bacterial/*chemistry/metabolism RNA, Molecular Nucleic Acid Conformation RNA Precursors/metabolism RNA, Transfer/metabolism Ribonuclease P/*chemistry/metabolism Thermus thermophilus/*chemistry/enzymology, Unité ARN, WESTHOF, X-Ray Evolution},
pubstate = {published},
tppubtype = {article}
}
Westhof E, Altman S
Three-dimensional working model of M1 RNA, the catalytic RNA subunit of ribonuclease P from Escherichia coli Journal Article
In: Proc Natl Acad Sci U S A, vol. 91, no. 11, pp. 5133-5137, 1994, ISBN: 7515186, (0027-8424 Journal Article).
Abstract | Links | BibTeX | Tags: Bacterial/*chemistry/metabolism RNA, Base Sequence Computer Graphics Computer Simulation Endoribonucleases/*chemistry/metabolism Escherichia coli/*enzymology Molecular Sequence Data *Nucleic Acid Conformation RNA, Catalytic/*chemistry/metabolism Ribonuclease P Substrate Specificity Support, Non-U.S. Gov't Support, P.H.S., U.S. Gov't, Unité ARN
@article{,
title = {Three-dimensional working model of M1 RNA, the catalytic RNA subunit of ribonuclease P from Escherichia coli},
author = {E Westhof and S Altman},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7515186},
isbn = {7515186},
year = {1994},
date = {1994-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {91},
number = {11},
pages = {5133-5137},
abstract = {A three-dimensional model of M1 RNA, the catalytic RNA subunit of RNase P from Escherichia coli, was constructed with the aid of a computer. The modeling process took into account data from chemical and enzymatic protection experiments, phylogenetic analysis, studies of the activities of mutants, and the kinetics of reactions catalyzed by the binding of substrate to M1 RNA. The model provides a plausible picture of the binding to M1 RNA of the tRNA domain of a precursor tRNA substrate. The scissile bond and adjacent segments of the aminoacyl acceptor stem of a precursor tRNA substrate can fit into a cleft that leads to the phylogenetically conserved, central part of the structure.},
note = {0027-8424
Journal Article},
keywords = {Bacterial/*chemistry/metabolism RNA, Base Sequence Computer Graphics Computer Simulation Endoribonucleases/*chemistry/metabolism Escherichia coli/*enzymology Molecular Sequence Data *Nucleic Acid Conformation RNA, Catalytic/*chemistry/metabolism Ribonuclease P Substrate Specificity Support, Non-U.S. Gov't Support, P.H.S., U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}