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Gene Review

ECs4226  -  tryptophanyl-tRNA synthetase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs4226


Psychiatry related information on ECs4226

  • Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease [3].

High impact information on ECs4226

  • Upon forming a complex, deiNOS quenches the fluorescence of an ATP analog bound to TrpRS II, and increases its affinity for substrate l-arginine [1].
  • Recombinantly expressed TrpRS II binds tryptophan (Trp), ATP, and D. radiodurans tRNA(Trp) and catalyzes the formation of 5' adenyl-Trp and tRNA(Trp), with approximately five times less activity than TrpRS I [1].
  • Aminoacylation in vitro by E. coli TrpRS of tRNA(Gln) transcripts mutated in the anticodon demonstrate that TrpRS recognizes all three nucleotides of the anticodon [4].
  • Steady-state kinetic analyses show that these mutant TrpRS proteins have increases in the apparent KM for tryptophan, decreases in turnover number, or both, without significant changes in the apparent KM for ATP or tRNA(Trp) [5].
  • Tryptophanyl-tRNA synthetase (TrpRS) is an interferon-induced phosphoprotein with autoantigenic and cytokine activities detected in addition to its canonical function in tRNA aminoacylation [3].

Chemical compound and disease context of ECs4226


Biological context of ECs4226

  • This high level of gene expression facilitates large scale preparation of TrpRS for physical studies, detection of in vivo degradation of mutant forms of TrpRS, and comparative assays of TrpRS by [3H]Trp-tRNA formation and by Trp-hydroxamate formation for the purpose of mutant characterization [6].

Other interactions of ECs4226


Analytical, diagnostic and therapeutic context of ECs4226

  • Protein sequence alignments revealed that A. ferrooxidans TrpRS contains a 70 amino acids long CP2 that is not found in any other bacterial TrpRS [2].
  • In immunoblotting, the 6C10 mAb reacts preferably with (i) oligomer than monomer, and (ii) bound than free TrpRS forms [3].
  • The effects of tRNA(Trp)variants on the aminoacylation reaction catalyzed by wild-type Escherichia coli tryptophanyl-tRNA synthe-tase (TrpRS) have now been investigated by stopped-flow fluorimetry, which allowed a pre-steady-state analysis to be undertaken [8].


  1. An unusual tryptophanyl tRNA synthetase interacts with nitric oxide synthase in Deinococcus radiodurans. Buddha, M.R., Keery, K.M., Crane, B.R. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  2. A dispensable peptide from Acidithiobacillus ferrooxidans tryptophanyl-tRNA synthetase affects tRNA binding. Zúñiga, R., Salazar, J., Canales, M., Orellana, O. FEBS Lett. (2002) [Pubmed]
  3. Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease. Paley, E.L., Smelyanski, L., Malinovskii, V., Subbarayan, P.R., Berdichevsky, Y., Posternak, N., Gershoni, J.M., Sokolova, O., Denisova, G. Mol. Immunol. (2007) [Pubmed]
  4. Switching tRNA(Gln) identity from glutamine to tryptophan. Rogers, M.J., Adachi, T., Inokuchi, H., Söll, D. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  5. Escherichia coli tryptophanyl-tRNA synthetase mutants selected for tryptophan auxotrophy implicate the dimer interface in optimizing amino acid binding. Sever, S., Rogers, K., Rogers, M.J., Carter, C., Söll, D. Biochemistry (1996) [Pubmed]
  6. High-level expression of Bacillus subtilis tryptophanyl-tRNA synthetase in Escherichia coli. Shi, W., Chow, K.C., Wong, J.T. Biochem. Cell Biol. (1990) [Pubmed]
  7. Synthesis of hybrid bisnucleoside 5',5"'-P1,P4-tetraphosphates by aminoacyl-tRNA synthetases. Traut, T.W. Mol. Cell. Biochem. (1987) [Pubmed]
  8. Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis. Ibba, M., Sever, S., Praetorius-Ibba, M., Söll, D. Nucleic Acids Res. (1999) [Pubmed]
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