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J Mol Biol. 2008 Sep 12;381(4):816-25. doi: 10.1016/j.jmb.2008.04.050. Epub 2008 Apr 29.

30 nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction.

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MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.


The mechanism by which chromatin is decondensed to permit access to DNA is largely unknown. Here, using a model nucleosome array reconstituted from recombinant histone octamers, we have defined the relative contribution of the individual histone octamer N-terminal tails as well as the effect of a targeted histone tail acetylation on the compaction state of the 30 nm chromatin fiber. This study goes beyond previous studies as it is based on a nucleosome array that is very long (61 nucleosomes) and contains a stoichiometric concentration of bound linker histone, which is essential for the formation of the 30 nm chromatin fiber. We find that compaction is regulated in two steps: Introduction of H4 acetylated to 30% on K16 inhibits compaction to a greater degree than deletion of the H4 N-terminal tail. Further decompaction is achieved by removal of the linker histone.

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