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. 2016 Jul 4;214(1):13–24. doi: 10.1083/jcb.201605005

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© 2016 Chen and Mellone

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — Overview of the stepwise assembly of histone proteins onto chromatin. (A) Nucleosomes form from H3-H4 dimer precursors, which associate with histone chaperones that prevent nonspecific histone–DNA interactions. These chaperones hand off histone dimers to assembly factors, which are specific to the histone they recognize. (B) The H3-H4 assembly factor is recruited to target chromatin regions by DNA-bound recruiter proteins, allowing the deposition of (H3-H4)₂ tetramers. (C) Upon the incorporation of H2A-H2B dimers, the new nucleosome forms. (D) The spacing of new and old particles that might have been altered during new histone deposition (disorganized nucleosomes) is restored by the chromatin remodeling activity of chromatin organizers (organized nucleosomes).