Reconstitution and Analysis of Hyperacetylated Chromatin

Specific acetylation at conserved lysines in the N-terminal tails of histones have been correlated with distinct chromatin structures, association of specific chromatin proteins, accessibility of nucleosomal DNA toward interaction of transcription factors, and unfolded chromatin with increased transcription potential (1 –5 ). Global histone acetylation prevents the folding of the nucleosomal fiber into higher order structures (6 ). Despite these correlations, the molecular principles governing molecular heterogeneity of chromatin structure and its implications for processes that require a DNA substrate are only poorly understood. But the close correlation between histone acetylation and gene activity suggests a contribution of histone acetylation (2 –4 ).