The interaction of RNA polymerase with histones.
Arginine-rich histones (F3) interact with both the bacterial and mammalian RNA polymerase and inhibit the in vitro RNA synthesis to a much greater extent than when associated with the DNA template. The lysine-rich histones (F1) inhibit the RNA synthesis mainly through template inhibition. Neither histone fraction displayed such an interaction with DNA polymerase. The RNA polymerase-F3 histone interaction takes place at ionic strength equal to or greater than those occurring in living cells, suggesting a possible role of arginine-rich histones in the regulation of RNA synthesis.
D000255:Adenosine Triphosphate; D001120:Arginine; D004254:DNA Nucleotidyltransferases; D006657:Histones; D008239:Lysine; D009994:Osmolar Concentration; D012313:RNA / Q000096:biosynthesis; D012316:RNA Nucleotidyltransferases; D013698:Templates, Genetic; D014316:Tritium
D006657:Histones; D014316:Tritium; D012313:RNA; D000255:Adenosine Triphosphate; D001120:Arginine; D004254:DNA Nucleotidyltransferases; D012316:RNA Nucleotidyltransferases; D008239:Lysine