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Glutamate-tRNAGln ligase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume S7)

Keywords

Escherichia Coli Bacillus Subtilis Zinc Acetate Unicellular Green Alga Acidithiobacillus Ferrooxidans 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    Schön, A.; Söl, D.: tRNA specificity of a mischarging aminoacyl-tRNA synthetase: glutamyl-tRNA synthetase from barley chloroplasts. FEBS Lett., 228, 241–244 (1988)CrossRefGoogle Scholar
  2. [2]
    Kim, S.I.; Soll, D.: Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl-tRNA synthetase. Mol. Cells, 8, 459–465 (1998)PubMedGoogle Scholar
  3. [3]
    Vothknecht, U.C.; Doernemann, D.: Charging of both, plastidial tRNAGlx and tRNAGlu with glutamate and subsequent amidation of the misacylated tRNAGln by a glutamyl-tRNA amidotransferase in the unicellular green alga Scenedesmus obliquus, mutant C-2A’. Z. Naturforsch. C, 50, 789–795 (1995)Google Scholar
  4. [4]
    Freist, W.; Gauss, D.H.; Soell, D.; Lapointe, J.: Glutamyl-tRNA synthetase. Biol. Chem., 378, 1313–1329 (1997)PubMedGoogle Scholar
  5. [5]
    Lapointe, J.; Duplain, L.; Proulx, M.: A single glutamyl-tRNA synthetase aminoacylates tRNAGlu and tRNAGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro. J. Bacteriol., 165, 88–93 (1986)PubMedGoogle Scholar
  6. [6]
    Pelchat, M.; Lacoste, L.; Yang, F.; Lapointe, J.: Overproduction of the Bacillus subtilis glutamyl-tRNA synthetase in its host and its toxicity to Escherichia coli. Can. J. Microbiol., 44, 378–381 (1998)CrossRefPubMedGoogle Scholar
  7. [7]
    Nunez, H.; Lefimil, C.; Min, B.; Soll, D.; Orellana, O.: In vivo formation of glutamyl-tRNA(Gln) in Escherichia coli by heterologous glutamyl-tRNA synthetases. FEBS Lett., 557, 133–135 (2004)CrossRefPubMedGoogle Scholar
  8. [8]
    Baick, J.W.; Yoon, J.H.; Namgoong, S.; Soll, D.; Kim, S.I.; Eom, S.H.; Hong, K.W.: Growth inhibition of Escherichia coli during heterologous expression of Bacillus subtilis glutamyl-tRNA synthetase that catalyzes the formation of mischarged glutamyl-tRNA1 Gln. J. Microbiol., 42, 111–116 (2004)PubMedGoogle Scholar
  9. [9]
    Lee, J.; Hendrickson, T.L.: Divergent anticodon recognition in contrasting glutamyl-tRNA synthetases. J. Mol. Biol., 344, 1167–1174 (2004)CrossRefPubMedGoogle Scholar
  10. [10]
    Salazar, J.C.; Ahel, I.; Orellana, O.; Tumbula-Hansen, D.; Krieger, R.; Daniels, L.; Soll, D.: Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates. Proc. Natl. Acad. Sci. USA, 100, 13863–13868 (2003)CrossRefPubMedGoogle Scholar
  11. [11]
    Schulze, J.O.; Masoumi, A.; Nickel, D.; Jahn, M.; Jahn, D.; Schubert, W.D.; Heinz, D.W.: Crystal structure of a non-discriminating glutamyl-tRNA synthetase. J. Mol. Biol., 361, 888–897 (2006)CrossRefPubMedGoogle Scholar

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