Histone acetylation in replication and transcription: Turnover at specific acetylation sites in histone H4 from Physarum polycephalum

Histone H4 from growing cells is partially acetylated at lysines 5, 8, 12, and 16. The turnover rate at each of these sites was investigated by pulse-labeling plasmodia of Physarum polycephalum with [ 3H]acetate for 55 min in either S phase or G2 phase of the cell cycle. Labeled histone H4 was purif...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1986-12, Vol.251 (2), p.665-673
Hauptverfasser:	Pesis, Karen H., Matthews, Harry R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Applied sciences Binding Sites Cell Cycle CHAMPIGNON Chromatography, High Pressure Liquid Exact sciences and technology FUNGI HISTONAS HISTONE HISTONES Histones - metabolism Interphase Nucleosomes - metabolism Other techniques and industries Peptide Fragments - analysis Physarum - genetics Physarum - metabolism PROTEASAS PROTEASE PROTEASES Transcription, Genetic
Online-Zugang:	Volltext
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