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Title: Effect of nonenzymatic histone acetylation on chromatin high-order folding. Author: Krajewski WA. Journal: Biochem Biophys Res Commun; 1996 Apr 16; 221(2):295-9. PubMed ID: 8619849. Abstract: In the present study we have made attempts to estimate the effect of histone acetylation on the folding of the chromatin fibril into its high-order structures. Histones were modified directly in isolated nuclei using acetyl adenylate as an acetyl donor. High-order folding of acetylated chromatin was analyzed by titration with increasing amounts of ethidium bromide. We have shown that chromatin with non-enzymatically acetylated histones exhibits a less folded conformation when compared to intact chromatin. We discuss the molecular bases of this phenomenon and propose a novel generalized model for regulation of chromatin high-order folding.[Abstract] [Full Text] [Related] [New Search]