Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

  title={Structural basis of translational control by Escherichia coli threonyl tRNA synthetase},
  author={Alfredo Torres-Larios and Anne-Catherine Dock-Br{\'e}geon and Pascale Romby and Bernard Rees and Rajan Sankaranarayanan and Joël Caillet and M. Springer and Chantal Ehresmann and Bernard Ehresmann and Dino Moras},
  journal={Nature Structural Biology},
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 modular structure of Escherichia coli threonyl‐tRNA synthetase as both an enzyme and a regulator of gene expression
A computer‐derived molecular model is constructed for the operator‐threonyl‐tRNA synthetase complex, which sheds light on several essential aspects of the regulatory mechanism.
Bacterial translational control at atomic resolution.
Translational Operator of mRNA on the Ribosome: How Repressor Proteins Exclude Ribosome Binding
The ribosome of Thermus thermophilus was cocrystallized with initiator transfer RNA (tRNA) and a structured messenger RNA (mRNA) carrying a translational operator to suggest a general way in which mRNA control elements must be placed on the ribosomes to perform their regulatory task.
Mutations in Residues Involved in Zinc Binding in the Catalytic Site of Escherichia coli Threonyl-tRNA Synthetase Confer a Dominant Lethal Phenotype
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Translational repression mechanisms in prokaryotes
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A threonyl-tRNA synthetase-mediated translation initiation machinery
It is found that, in vertebrate, threonyl-tRNA synthetase (TRS) can act as a scaffold for the initiation machinery to stimulate the translation of a specific set of mRNAs.
Noncanonical functions of aminoacyl-tRNA synthetases
In this review, recent data on the noncanonical functions of aminoacyl-tRNA synthetases are summarized and the mechanisms of their action are summarized.
A domain for editing by an archaebacterial tRNA synthetase.
Results demonstrate a domain for editing that is distinct from all others, is restricted to just one branch of the tree of life, and was most likely added to archaebacterial ThrRSs after the eukaryote/archaebacteria split.
Aminoacyl-tRNA Synthetases.
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The specificity of translational control switched with transfer RNA identity rules.
A mutation suggested by tRNA identity rules that switches the resemblance of the leader sequence from tRNA(Thr) to t RNA(Met) causes the translation of the threonyl-tRNA synthetase messenger RNA to become regulated by methionyl-tRNAs.
Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli.
Findings suggest that the tRNAThr ligase regulates its translation by binding to its mRNA at a place that shares some homology with its natural substrate.
The expression of E.coli threonyl‐tRNA synthetase is regulated at the translational level by symmetrical operator‐repressor interactions.
In vitro and in vivo evidence is provided that two stemloop structures are recognized by the enzyme in an analogous way and mimic the anticodon arm of E.coli tRNA(Thr), stressing the importance of such interactions in translational regulation of gene expression.
tRNA‐like structures and gene regulation at the translational level: a case of molecular mimicry in Escherichia coli.
The observed correlation between regulatory and aminoacylation defects strongly suggests that the synthetase recognizes the similar parts of its two RNA ligands‐‐the anticodon‐like arm of the mRNA and the true anticodon arm ofThe tRNA‐‐in an analogous way.
The structure of an AspRS—tRNAAsp complex reveals a tRNA‐dependent control mechanism
The 2.6 Å resolution crystal structure of an inactive complex between yeast tRNAAsp and Escherichia coli aspartyl‐tRNA synthetase reveals the molecular details of a tRNA‐induced mechanism that
The Escherichia coli threonyl‐tRNA synthetase gene contains a split ribosomal binding site interrupted by a hairpin structure that is essential for autoregulation
It is shown that the ribosome binds to thrS mRNA at two non‐contiguous sites: region −12 to +16 comprising the SD sequence and the AUG codon and, unexpectedly, an upstream single‐stranded sequence in domain 3.