Abstract

The core histone tail domains are known to be key regulators of chromatin structure and function. The tails are required for condensation of nucleosome arrays into secondary and tertiary chromatin structures, yet little is known regarding tail structures or sites of tail interactions in chromatin. We have developed a system to test the hypothesis that the tails participate in internucleosomal interactions during salt-dependent chromatin condensation, and here we used it to examine interactions of the H3 tail domain. We found that the H3 tail participates primarily in intranucleosome interactions when the nucleosome array exists in an extended "beads-on-a-string" conformation and that tail interactions reorganize to engage in primarily internucleosome interactions as the array successively undergoes salt-dependent folding and oligomerization. These results indicated that the location and interactions of the H3 tail domain are dependent upon the degree of condensation of the nucleosomal array, suggesting a mechanism by which alterations in tail interactions may elaborate different structural and functional states of chromatin.

Highlights

  • The core histone tail domains are essential for compaction of oligonucleosome arrays into secondary chromatin structures and for efficient assembly of oligomeric tertiary structures (1, 2, 8 –10)

  • We wished to determine whether the H3 tail domain contacts the DNA of neighboring nucleosomes and whether these interactions are dependent upon condensation of the nucleosome array

  • Our experimental scheme to investigate internucleosomal interactions during salt-dependent condensation of the model nucleosome array is depicted in Fig. 1, First, a mononucleosome (N1) containing a site- modified H3 tail domain was ligated to the end of a 12-mer nucleosome array preassembled with native chicken erythro

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Summary

Introduction

The core histone tail domains are essential for compaction of oligonucleosome arrays into secondary chromatin structures and for efficient assembly of oligomeric tertiary structures (1, 2, 8 –10). Our experimental scheme to investigate internucleosomal interactions during salt-dependent condensation of the model nucleosome array is depicted, First, a mononucleosome (N1) containing a site- modified H3 tail domain was ligated to the end of a 12-mer nucleosome array preassembled with native chicken erythro-

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