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Histone acetyltransferase activity during the cell cycle.

G Golderer1, P Loidl, P Gröbner

  • 1Institut für Medizinische Chemie und Biochemie der Universität, Innsbruck, Austria.

FEBS Letters
|October 5, 1987
PubMed
Summary

Histone acetyltransferase activity in Physarum polycephalum shows cell cycle periodicity, peaking in early G2. Enzyme activity alone does not fully explain in vivo histone acetylation patterns.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Histone acetylation regulates gene expression and chromatin structure.
  • Understanding cell cycle-dependent epigenetic modifications is crucial for cell biology research.
  • Physarum polycephalum offers a model for synchronous cell cycle studies.

Purpose of the Study:

  • To investigate the cell cycle-dependent activity of histone acetyltransferase (HAT) in Physarum polycephalum.
  • To compare in vitro HAT activity with in vivo histone acetylation patterns during the cell cycle.
  • To identify factors influencing histone acetylation during the cell cycle.

Main Methods:

  • Isolated nuclei from synchronous Physarum polycephalum cultures were used.
  • Histone acetyltransferase activity was measured using [14C]acetyl-coenzyme A and exogenous calf thymus histones.
  • Enzyme activity was quantified across different phases of the cell cycle.

Main Results:

  • Histone acetyltransferase activity exhibited clear periodicity throughout the cell cycle.
  • Activity increased during S-phase, peaked in early G2, and declined in mid-to-late G2.
  • The observed enzyme activity pattern did not fully account for in vivo histone acetylation.

Conclusions:

  • Histone acetyltransferase activity is cell cycle-regulated in Physarum polycephalum.
  • Other factors, potentially related to chromatin structure, modulate in vivo histone acetylation.
  • This study highlights the complexity of epigenetic regulation during the cell cycle.

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