Abstract
We characterized the effect of histone acetylation on the structure of a nucleosome and the interactions between two nucleosomes from a single molecule approach. In this study, histones in nucleosomes were acetylated with a histone acetyltransferase enzyme that acetylates mainly H2A and H4 N-terminal tails. Based on single molecule fluorescence measurements, we observed directional unwrapping of nucleosomal DNA upon histone acetylation in a sequence-dependent manner. In addition, interactions between two nucleosomes in solution yield multiple transient dinucleosomal states which can be categorized to short-lived and long-lived states. Unacetylated nucleosomes favor the formation of long-lived dinucleosomes 4-fold as much as the acetylated ones. These results indicate that the acetylation of histone H2A/H4 tails alters the structure of nucleosomes and the interactions between nucleosomes. We also suggest a model for the structure of a dinucleosome based on our experimental data. These results deepen our understanding of the effect of histone acetylation on the structure of chromatin.
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