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Related Experiment Videos

Coupling between catalysis and oligomeric structure in nucleoside diphosphate kinase

S Mesnildrey1, F Agou, A Karlsson

  • 1Unité de Régulation Enzymatique des Activités Cellulaires Institut Pasteur, CNRS URA 1149, 25 rue du Docteur Roux, 75724 Paris, Cedex 15, France.

The Journal of Biological Chemistry
|March 21, 1998
PubMed
Summary

A mutated Dictyostelium nucleoside diphosphate kinase (NDPK) was stabilized in a dimeric form. Nucleotide substrates induced its reassociation into an active hexamer, suggesting distinct oligomeric states serve varied cellular roles.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Dictyostelium nucleoside diphosphate kinase (NDPK) is crucial for cellular processes.
  • Wild-type NDPK typically exists as a hexamer.
  • Understanding NDPK oligomerization is key to its function.

Purpose of the Study:

  • To stabilize a dimeric form of Dictyostelium NDPK.
  • To investigate the role of oligomeric state in NDPK enzymatic activity.
  • To explore the mechanism of NDPK reassociation.

Main Methods:

  • Site-directed mutagenesis to create a stable dimeric mutant (P100S-N150stop).
  • Biophysical techniques including equilibrium sedimentation and gel filtration.
  • Enzymatic activity assays to measure kinase function.

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Main Results:

  • The P100S-N150stop mutation successfully stabilized a dimeric NDPK form.
  • Dimeric NDPK was enzymatically inactive.
  • Nucleotide substrates induced the reassociation of dimeric NDPK into an active hexamer.
  • Enzyme reactivation correlated with reassociation into the hexameric form.

Conclusions:

  • NDPK exists in different oligomeric states, including an inactive dimer and an active hexamer.
  • Nucleotide binding triggers the transition from inactive dimer to active hexamer.
  • Inactive dimeric NDPK may play roles in cellular processes independent of enzymatic activity.