@article{,
title = {Structural basis of translational control by Escherichia coli threonyl tRNA synthetase},
author = {A Torres-Larios and A C Dock-Bregeon and P Romby and B Rees and R Sankaranarayanan and J Caillet and M Springer and C Ehresmann and B Ehresmann and D Moras},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11953757},
isbn = {11953757},
year = {2002},
date = {2002-01-01},
journal = {Nat Struct Biol},
volume = {9},
number = {5},
pages = {343-347},
abstract = {Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to the enzyme surface. The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-negative bacteria.},
note = {1072-8368
Journal Article},
keywords = {Anticodon/genetics Base Sequence Crystallography, Bacterial/chemistry/genetics/metabolism RNA, Genetic, Messenger/chemistry/genetics/*metabolism RNA, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Conformation RNA, Non-U.S. Gov't Threonine-tRNA Ligase/*chemistry/*metabolism *Translation, ROMBY, Transfer/chemistry/genetics/metabolism Sequence Alignment Structure-Activity Relationship Support, Unité ARN, X-Ray Escherichia coli/*enzymology/genetics Models},
pubstate = {published},
tppubtype = {article}
}
Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to the enzyme surface. The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-negative bacteria.