Aspartyl-tRNA Synthetase-Induced Aspartylation of Proteins: a Fingerprint Approach to Map Accessible Domains in Protein

  • H. Mejdoub
  • D. Kern
  • R. Giege
  • Y. Boulanger
  • J. Reinbolt


Aspartic acid can be covalently linked to yeast aspartyl-tRNA synthetase and to other proteins in the absence of tRNA, under conditions where the synthetase activates the amino acid into aspartyl-adenylate, i.e., in the presence of ATP and MgCl2 [1,2]. The aspartyl adenylate is poorly bound to the enzyme.


Aspartic Acid Degradation Step Aspartic Acid Residue Amino Alcohol Label Peptide 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • H. Mejdoub
    • 1
  • D. Kern
    • 1
  • R. Giege
    • 1
  • Y. Boulanger
    • 1
  • J. Reinbolt
    • 1
  1. 1.Institut de Biologie Moléculaire et Cellulaire du C.N.R.S.Laboratoire de BiochimieStrasbourgFrance

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