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Post-translational processing of Drosophila nucleoside diphosphate kinase.

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Author

Summary, in English

Nucleoside diphosphate kinase (NDPK) was purified from Drosophila melanogaster by a combination of anion-exchange, hydroxyapatite, and reversed-phase chromatography. The identity of the purified enzyme was confirmed by sequencing internal peptides (the N-terminus appeared to be blocked). Post-translational modifications were investigated by using protein chemical and mass spectrometric methods. Analysis by nanoelectrospray ionization-mass spectrometry revealed that the mass of the enzyme was considerably smaller than that predicted from its amino acid sequence. Although its open-reading frame predicts a 153-residue polypeptide, the mature enzyme was found to comprise 152 amino acids, being modified by proteolytic removal of the initiator Met and N-acetylation of Ala2. This explains why the observed pI of the Drosophila enzyme is more acidic than that predicted from its amino acid sequence. No additional post-translational modifications such as glycosylation or O-phosphorylation, which have been identified on homologous NDPKs from other organisms, were detected on the Drosophila enzyme.

Publishing year

2002

Language

English

Pages

689-694

Publication/Series

Biochemical and Biophysical Research Communications

Volume

295

Issue

3

Document type

Journal article

Publisher

Elsevier

Topic

  • Biological Sciences

Keywords

  • Drosophila melanogaster : enzymology
  • Durapatite : pharmacology
  • Glycosylation
  • Nucleoside-Diphosphate Kinase : chemistry
  • Nucleoside-Diphosphate Kinase : isolation & purification
  • Open Reading Frames
  • Peptides : chemistry
  • Phosphorylation
  • Protein Processing
  • Spectrum Analysis
  • Post-Translational
  • Mass
  • Ion Exchange
  • Chromatography
  • Biocompatible Materials : pharmacology
  • Animal

Status

Published

Research group

  • Clinical Chemistry, Malmö

ISBN/ISSN/Other

  • ISSN: 1090-2104