(Lysyl-Glycyl-Glycyl)5 and (Lysyl-Glycyl-Glycyl)10 as models of histone. Interaction with DNA and acetylation by calf thymus enzyme.
Sequential polypeptides (Lys-Gly-Gly)5 and (Lys-Gly-Gly)10 were synthesized as models for the N-terminal region of H4 histone and their interactions with DNA were studied. The ability of (Lys-Gly-Gly)10 to precipitate DNA was found to be much higher than that of (Lys-Gly-Gly)5. For example, at the physiological salt concentration, (Lys-Gly-Gly)10 precipitates DNA but (Lys-Gly-Gly)5 does not. Both peptides could be acetylated by a partially purified histone acetyltransferase preparation derived from calf thymus. epsilon-Amino groups of lysyl residues were the sites of the acetylation. DNA-cellulose chromatography of the products indicated that acetylation weakened the interaction of the peptides with DNA.
D000107:Acetylation; D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D004247:DNA / Q000378:metabolism*; D005998:Glycine; D006657:Histones / Q000378:metabolism*; D008239:Lysine; D009994:Osmolar Concentration; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism*; D013950:Thymus Gland / Q000201:enzymology
D006657:Histones; D010455:Peptides; D004247:DNA; D000217:Acyltransferases; D008239:Lysine; D005998:Glycine