Abstract
Publisher Summary The chapter highlights that the H4 N-terminal tail plays a pivotal role in compaction of the array. While electrostatic interactions between the histone tails and DNA clearly contribute to tail-directed folding of the chromatin fiber, the special role of the H4 tail may be due to H4 interactions with an H2A–H2B dimer within adjacent nucleosomes. This chapter presents a technique to study internucleosome protein–DNA interactions in a model dinucleosome system. Model dinucleosomes are generated in which one nucleosome typically contains a radiolabeled DNA template and native histones, whereas the other contains a single histone site specifically modified with a UV-activatable cross-linking agent. Each of the nucleosomes is reconstituted independently and then ligated together, and cross-linking is induced by UV irradiation under various conditions. After cross-linking, the two DNA templates are separated so that internucleosomal histone–DNA cross-links can be distinguished from intranucleosomal cross-links. In addition, the chapter describes a novel method for the preparation of H3-H4 tetramers.
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