Transcribing chromatin is not preferentially enriched with acetylated histones.
Chromatin fragments of the RNA polymerase II-transcriptional complex were purified from the micrococcal nuclease digest of rat liver nuclei in the presence of n-butyrate, a potent histone deacetylase inhibitor. Polyacrylamide gel electrophoretic analysis in Triton acid-urea revealed that the extent of histone acetylation of the complex did not differ markedly from that of the total chromatin.
D000107:Acetylation; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002843:Chromatin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000201:enzymology / Q000378:metabolism*; D012319:RNA Polymerase II / Q000302:isolation & purification; D051381:Rats; D014158:Transcription, Genetic
D002843:Chromatin; D006657:Histones; D012319:RNA Polymerase II