Structural basis for tRNA-dependent amidotransferase function.

@article{Schmitt2005StructuralBF,
  title={Structural basis for tRNA-dependent amidotransferase function.},
  author={E. Schmitt and M. Panvert and S. Blanquet and Y. Mechulam},
  journal={Structure},
  year={2005},
  volume={13 10},
  pages={
          1421-33
        }
}
Besides direct charging of tRNAs by aminoacyl-tRNA synthetases, indirect routes also ensure attachment of some amino acids onto tRNA. Such routes may explain how new amino acids entered into protein synthesis. In archaea and in most bacteria, tRNA(Gln) is first misaminoacylated by glutamyl-tRNA synthetase. Glu-tRNA(Gln) is then matured into Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. We report the structure of a tRNA-dependent amidotransferase-that of GatDE from Pyrococcus abyssi. The 3… Expand
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TLDR
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References

SHOWING 1-10 OF 43 REFERENCES
Domain-specific recruitment of amide amino acids for protein synthesis
TLDR
It is shown that all archaea possess an archaea-specific heterodimeric amidotransferase (encoded by gatD and gatE) for Gln-tRNA formation, providing direct evidence for a relationship between amino-acid metabolism and protein biosynthesis. Expand
Protein biosynthesis in organelles requires misaminoacylation of tRNA
TLDR
It appears that the occurrence of this pathway of Gln-tRNAGln formation is widespread among organisms and is a function conserved during evolution, which raises questions about the origin of organelles and about the evolution of the mechanisms maintaining accuracy in protein biosynthesis. Expand
Widespread Use of the Glu-tRNAGln Transamidation Pathway among Bacteria
TLDR
A revisited model for the evolution of the contemporary glutamyl-tRNA synthetases and glutaminyl- tRNA synthenases that differs from the generally accepted model forthe evolution of aminoacyl-t RNA synthetase is proposed. Expand
Gln-tRNAGln Formation from Glu-tRNAGln Requires Cooperation of an Asparaginase and a Glu-tRNAGln Kinase*
TLDR
It is shown here that Methanothermobacter thermautotrophicus GatD acts as a glutaminase but only in the presence of both Glu-tRNAGln and the other subunit, GatE, and that GatE alone could form the intermediate, which may point to an ancient link between glutamine synthesized for metabolism and translation. Expand
Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis.
TLDR
Examination of the preliminary genomic sequence of the radiation-resistant bacterium Deinococcus radiodurans suggests the presence of both direct and indirect routes of Asn-tRNA and Gln- tRNA formation, and suggests that the gatCAB genes may be responsible for biosynthesis ofAsparagine in this asparagine prototroph. Expand
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase.
TLDR
Tight coupling among ATP or ATP-gammaS hydrolysis and glutaminase and transamidase activities reveals tight coupling among these activities in the presence of ATP, with all three activities waning in concert when Glu-tRNA(Gln) levels become exhausted. Expand
γ-Glutamyl Phosphate Attached to Glutamine-Specific tRNA
B. subtilis Gln-tRNA formation, in vitro, involves the initial acceptance of glutamic acid by tRNAGln to form a missense Glu-tRNAGln intermediate which is converted to Gln-tRNA by a subsequentExpand
Synthesis of aspartyl‐tRNAAsp in Escherichia coli—a snapshot of the second step
TLDR
Two archetypal RNA–protein modes of interactions are observed: the anticodon stem–loop, including the wobble base Q, binds to the N‐terminal β‐barrel domain through direct protein–RNA interactions, while the binding of the acceptor stem involves both direct and water‐mediated hydrogen bonds in an original recognition scheme. Expand
Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.
  • A. Curnow, K. Hong, +5 authors D. Söll
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1997
TLDR
It is demonstrated that transamidation is the only pathway to Gln-t RNAGln in B. subtilis and that glutamyl-tRNAGln amidotransferase is a novel and essential component of the translational apparatus. Expand
Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways.
  • H. Becker, D. Kern
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1998
TLDR
Findings shed light on the interrelation between the t RNA-dependent and tRNA-independent pathways of amino acid amidation and on the processes involved in fidelity of the aminoacylation systems. Expand
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