Abstract
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).
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© 1999 Humana Press Inc.
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Krajewski, W.A., Becker, P.B. (1999). Reconstitution and Analysis of Hyperacetylated Chromatin. In: Becker, P.B. (eds) Chromatin Protocols. Methods in Molecular Biology™, vol 119. Humana Press. https://doi.org/10.1385/1-59259-681-9:207
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DOI: https://doi.org/10.1385/1-59259-681-9:207
Publisher Name: Humana Press
Print ISBN: 978-0-89603-665-9
Online ISBN: 978-1-59259-681-2
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