Control of histone acetylation cell cycle dependence of deacetylase activity in physarum polycephalum nuclei
Waterborg, J.H.; Matthews, H.R.
Experimental Cell Research 138(2): 462-466
1982
ISSN/ISBN: 0014-4827
Accession: 005050086
Nuclei from naturally synchronous plasmodia of P. 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. Evidently, H4 acetylation is linked to prior chromatin structural changes.