These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • 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]