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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.

Author information

1
From the Department of Biochemistry and Biophysics, University of Rochester, Rochester, New York 14642.
2
From the Department of Biochemistry and Biophysics, University of Rochester, Rochester, New York 14642 Jeffrey_Hayes@urmc.rochester.edu.

Abstract

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.

KEYWORDS:

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

PMID:
25122771
PMCID:
PMC4175364
DOI:
10.1074/jbc.M114.595140
[Indexed for MEDLINE]
Free PMC Article
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