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Related Experiment Videos

NAP-2: histone chaperone function and phosphorylation state through the cell cycle.

P Rodriguez1, J Pelletier, G B Price

  • 1McGill Cancer Center, Montreal, Quebec, Canada.

Journal of Molecular Biology
|April 15, 2000
PubMed
Summary
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Casein kinase 2 (CKII) phosphorylates nucleosome assembly proteins (NAP-1 and NAP-2). NAP-2 phosphorylation regulates its cell cycle-dependent nuclear transport, influencing histone chaperone activity.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nucleosome assembly proteins (NAP-1 and NAP-2) are crucial for chromatin dynamics.
  • The role of post-translational modifications, such as phosphorylation, in regulating NAP function is not fully understood.

Purpose of the Study:

  • To investigate the interaction between casein kinase 2 (CKII) and nucleosome assembly proteins (NAP-1 and NAP-2).
  • To determine the cell-cycle-dependent phosphorylation status of NAP-2 and its impact on nuclear localization and histone binding.

Main Methods:

  • In vitro kinase assays using immobilized NAP-2 and HeLa cell nuclear extracts.
  • Inhibition studies using heparin, a CKII specific inhibitor.
  • Analysis of NAP-2 phosphorylation and localization in vivo using cell extracts and indirect immunofluorescence.

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Main Results:

  • CKII directly phosphorylates both NAP-1 and NAP-2 in vitro.
  • Heparin abolished NAP-1 and NAP-2 phosphorylation in crude extracts, confirming CKII's role.
  • Core histones stimulated CKII-mediated phosphorylation of NAP-1 and NAP-2.
  • NAP-2 is phosphorylated at the G0/G1 boundary but not during S-phase.
  • Phosphorylated NAP-2 resides in the cytoplasm with histones, while dephosphorylation triggers nuclear import at the G1/S boundary.
  • NAP-2 localization during metaphase is distinct from chromosomes.

Conclusions:

  • CKII is a key kinase regulating NAP-2 phosphorylation.
  • NAP-2 phosphorylation status controls its cell-cycle distribution and nuclear transport.
  • NAP-2 functions as a histone chaperone throughout the cell cycle, with its localization dictated by phosphorylation.