The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

aspS  -  aspartyl-tRNA synthetase

Escherichia coli O157:H7 str. Sakai

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of ECs2576

  • We have explored here the human mt-aspartate system in which a prokaryotic-type AspRS, highly similar to the Escherichia coli enzyme, recognizes a bizarre tRNA(Asp) [1].
  • Here, we report the first characterization of the ND-AspRS from the human pathogen Helicobacter pylori (H. pylori or Hp) [2].
  • The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity [2].
 

High impact information on ECs2576

  • These three latter aaRS share three new sequence motifs with AspRS, AsnRS, LysRS, HisRS and the beta subunit of PheRS [3].
  • Primary sequence- and 3D-based phylogeny shows that an archaeal AspRS ancestor originated AS-AR, which was subsequently transferred into bacteria by lateral gene transfer in which it underwent structural changes producing AS-A [4].
  • Replacing this glycine by an aspartate renders human mt-AspRS more discriminative to G73 [1].
  • The product of degradation, a modified aspartyl-adenylate containing an N-acylphosphoramidate linkage, strongly inhibits translation by blocking the function of aspartyl-tRNA synthetase [5].
  • This water-assisted asparagine recognition by the AsnRS strikingly contrasts with the fact that the aspartic acid recognition by the closely related aspartyl-tRNA synthetase is achieved exclusively through extensive interactions with protein amino acid residues [6].
 

Biological context of ECs2576

  • The mutated AspRS purified from an overproducing strain displayed marked temperature sensitivity, with half-life values of 22 and 68 min (at 42 degrees C), respectively, for tRNA aminoacylation and ATP/PPi exchange activities [7].
 

Associations of ECs2576 with chemical compounds

  • In other bacteria, particularly those that lack AsnRS, AspRS is nondiscriminating (ND-AspRS) and generates both Asp-tRNA(Asp) and the noncanonical, misacylated Asp-tRNA(Asn); this misacylated tRNA is subsequently repaired by the glutamine-dependent Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase (Asp/Glu-Adt) [2].

References

  1. Loss of a primordial identity element for a mammalian mitochondrial aminoacylation system. Fender, A., Sauter, C., Messmer, M., Pütz, J., Giegé, R., Florentz, C., Sissler, M. J. Biol. Chem. (2006) [Pubmed]
  2. The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity. Chuawong, P., Hendrickson, T.L. Biochemistry (2006) [Pubmed]
  3. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Eriani, G., Delarue, M., Poch, O., Gangloff, J., Moras, D. Nature (1990) [Pubmed]
  4. When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism. Roy, H., Becker, H.D., Reinbolt, J., Kern, D. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  5. Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic Microcin C. Metlitskaya, A., Kazakov, T., Kommer, A., Pavlova, O., Praetorius-Ibba, M., Ibba, M., Krasheninnikov, I., Kolb, V., Khmel, I., Severinov, K. J. Biol. Chem. (2006) [Pubmed]
  6. Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase. Iwasaki, W., Sekine, S., Kuroishi, C., Kuramitsu, S., Shirouzu, M., Yokoyama, S. J. Mol. Biol. (2006) [Pubmed]
  7. Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant. Martin, F., Sharples, G.J., Lloyd, R.G., Eiler, S., Moras, D., Gangloff, J., Eriani, G. J. Bacteriol. (1997) [Pubmed]
 
WikiGenes - Universities