Control of histone acetylation: Cell-cycle dependence of deacetylase activity in Physarum nuclei

Nuclei from naturally synchronous plasmodia of Physarum polycephalum were assayed for histone deacetylase activity. The substrate for the assay was a peptide comprising the amino terminal region (residues 1–23) of calf thymus histone H4. The deacetylase activity per nucleus remained constant during...

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Veröffentlicht in:Experimental cell research 1982-01, Vol.138 (2), p.462-466
Hauptverfasser: Waterborg, Jaap H., Matthews, Harry R.
Format: Artikel
Sprache:eng
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Zusammenfassung:Nuclei from naturally synchronous plasmodia of Physarum polycephalum were assayed for histone deacetylase activity. The substrate for the assay was a peptide comprising the amino terminal region (residues 1–23) of calf thymus histone H4. The deacetylase activity per nucleus remained constant during S phase and early G2 phase and then doubled in a linear fashion during mid and late G2 phase reaching its maximum level at metaphase. The data imply that H4 acetylation is linked to prior chromatin structural changes.
ISSN:0014-4827
1090-2422
DOI:10.1016/0014-4827(82)90200-2