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Gene Review

aspC  -  aspartyl-tRNA synthetase

Thermococcus kodakarensis KOD1

 
 
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Disease relevance of TK0492

 

High impact information on TK0492

  • Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation [2].
  • We attempted to expand the tRNA recognition of the discriminating Thermococcus kodakaraensis AspRS to that of a ND-AspRS by in vitro mutagenesis [3].
  • In contrast, a discriminating AspRS cannot acylate tRNA(Asn) [4].
  • The mischarging AspRS correlates with the absence in the genome of AsnRS and the presence of Asp-tRNA(Asn) amidotransferase, employed by the transamidation pathway [4].
  • In contrast, the discriminating AspRS correlates with the absence of the amidotransferase and the presence of AsnRS, forming Asn-tRNA by direct aminoacylation [4].
 

Biological context of TK0492

  • Analysis of the deduced amino-acid sequence (438 aa, 50,893 Da) revealed that the AspRS of KOD1 is a chimerical protein of bacteria and eukarya [1].

References

  1. Aspartyl-tRNA synthetase of the hyperthermophilic archaeon Pyrococcus sp. KOD1 has a chimerical structure of eukaryotic and bacterial enzymes. Imanaka, T., Lee, S., Takagi, M., Fujiwara, S. Gene (1995) [Pubmed]
  2. Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation. Schmitt, E., Moulinier, L., Fujiwara, S., Imanaka, T., Thierry, J.C., Moras, D. EMBO J. (1998) [Pubmed]
  3. Expanding tRNA recognition of a tRNA synthetase by a single amino acid change. Feng, L., Tumbula-Hansen, D., Toogood, H., Soll, D. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms. Tumbula-Hansen, D., Feng, L., Toogood, H., Stetter, K.O., Söll, D. J. Biol. Chem. (2002) [Pubmed]
 
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