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 |
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| container_title | Experimental cell research |
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| creator | Waterborg, Jaap H. Matthews, Harry R. |
| description | 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. |
| doi_str_mv | 10.1016/0014-4827(82)90200-2 |
| format | Article |
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| ispartof | Experimental cell research, 1982-01, Vol.138 (2), p.462-466 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Acetylation Amidohydrolases - metabolism Cell Cycle Cell Nucleus - analysis Histone Deacetylases - metabolism Histones - metabolism Physarum - metabolism Physarum polycephalum |
| title | Control of histone acetylation: Cell-cycle dependence of deacetylase activity in Physarum nuclei |
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