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J Biol Chem. 2014 Sep 26;289(39):27342-51. doi: 10.1074/jbc.M114.595140. Epub 2014 Aug 13.

A distinct switch in interactions of the histone H4 tail domain upon salt-dependent folding of nucleosome arrays.

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From the Department of Biochemistry and Biophysics, University of Rochester, Rochester, New York 14642.
From the Department of Biochemistry and Biophysics, University of Rochester, Rochester, New York 14642


The core histone tail domains mediate inter-nucleosomal interactions that direct folding and condensation of nucleosome arrays into higher-order chromatin structures. The histone H4 tail domain facilitates inter-array interactions by contacting both the H2A/H2B acidic patch and DNA of neighboring nucleosomes. Likewise, H4 tail-H2A contacts stabilize array folding. However, whether the H4 tail domains stabilize array folding via inter-nucleosomal interactions with the DNA of neighboring nucleosomes remains unclear. We utilized defined oligonucleosome arrays containing a single specialized nucleosome with a photo-inducible cross-linker in the N terminus of the H4 tail to characterize these interactions. We observed that the H4 tail participates exclusively in intra-array interactions with DNA in unfolded arrays. These interactions are diminished during array folding, yet no inter-nucleosome, intra-array H4 tail-DNA contacts are observed in condensed chromatin. However, we document contacts between the N terminus of the H4 tail and H2A. Installation of acetylation mimics known to disrupt H4-H2A surface interactions did not increase observance of H4-DNA inter-nucleosomal interactions. These results suggest the multiple functions of the H4 tail require targeted distinct interactions within condensed chromatin.


Chromatin; Chromatin Regulation; Chromatin Structure; Higher-order Chromatin Structure; Histone; Histone Tail Domain; Nucleosome

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